Structure and function of archaeal box C/D sRNP core proteins

Nop56p and Nop58p are two core proteins of the box C/D snoRNPs that interact concurrently with fibrillarin and snoRNAs to function in enzyme assembly and catalysis. Here we report the 2.9 Å resolution co-crystal structure of an archaeal homolog of Nop56p/Nop58p, Nop5p, in complex with fibrillarin fr...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Nature Structural Biology 2003-04, Vol.10 (4), p.256-263
Hauptverfasser: Aittaleb, Mohamed, Rashid, Rumana, Chen, Qiong, Palmer, John R., Daniels, Charles J., Li, Hong
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 263
container_issue 4
container_start_page 256
container_title Nature Structural Biology
container_volume 10
creator Aittaleb, Mohamed
Rashid, Rumana
Chen, Qiong
Palmer, John R.
Daniels, Charles J.
Li, Hong
description Nop56p and Nop58p are two core proteins of the box C/D snoRNPs that interact concurrently with fibrillarin and snoRNAs to function in enzyme assembly and catalysis. Here we report the 2.9 Å resolution co-crystal structure of an archaeal homolog of Nop56p/Nop58p, Nop5p, in complex with fibrillarin from Archaeoglobus fulgidus (AF) and the methyl donor S -adenosyl- L -methionine. The N-terminal domain of Nop5p forms a complementary surface to fibrillarin that serves to anchor the catalytic subunit and to stabilize cofactor binding. A coiled coil in Nop5p mediates dimerization of two fibrillarin–Nop5p heterodimers for optimal interactions with bipartite box C/D RNAs. Structural analysis and complementary biochemical data demonstrate that the conserved C-terminal domain of Nop5p harbors RNA-binding sites. A model of box C/D snoRNP assembly is proposed based on the presented structural and biochemical data.
doi_str_mv 10.1038/nsb905
format Article
fullrecord <record><control><sourceid>proquest_osti_</sourceid><recordid>TN_cdi_proquest_miscellaneous_73140172</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>73140172</sourcerecordid><originalsourceid>FETCH-LOGICAL-c459t-a8787108973bce4fc8e7ed05b0cdc89a18cf365ab17cf3b0c058796ba661c89c3</originalsourceid><addsrcrecordid>eNqFkV1LwzAUhoMoTqf-BCkKelWXtE2TXHgh8xOGih_XIT1LXUeXzCQF_fdGOhzsxqscch6enJMXoSOCLwjO-cj4SmC6hfYILWgqBKfbf7XIB2jf-znGGaUs30UDklHBucj20OVrcB2EzulEmWlSdwZCY01i60Q5mCmt2qSyX8l4dJ34l8fnBGxEl84G3Rh_gHZq1Xp9uDqH6P325m18n06e7h7GV5MUCipCqjjjjGAuWF6BLmrgmukpphWGKXChCIc6L6mqCItFvMWUM1FWqixJ7EM-RKe91_rQSA9N0DADa4yGIAnFOOqLSJ31VBzvs9M-yEXjQbetMtp2XrKcFJiw7F-QcI5zEv9tiE42wLntnImryizjmSg4Kdc2cNZ7p2u5dM1CuW9JsPwNR_bhRPB4ZeuqhZ6usVUaETjvAR9b5kO79XMbqh9wU5Rw</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>228294816</pqid></control><display><type>article</type><title>Structure and function of archaeal box C/D sRNP core proteins</title><source>MEDLINE</source><source>Nature</source><source>Springer Nature - Complete Springer Journals</source><creator>Aittaleb, Mohamed ; Rashid, Rumana ; Chen, Qiong ; Palmer, John R. ; Daniels, Charles J. ; Li, Hong</creator><creatorcontrib>Aittaleb, Mohamed ; Rashid, Rumana ; Chen, Qiong ; Palmer, John R. ; Daniels, Charles J. ; Li, Hong ; Brookhaven National Laboratory, National Synchrotron Light Source (US)</creatorcontrib><description>Nop56p and Nop58p are two core proteins of the box C/D snoRNPs that interact concurrently with fibrillarin and snoRNAs to function in enzyme assembly and catalysis. Here we report the 2.9 Å resolution co-crystal structure of an archaeal homolog of Nop56p/Nop58p, Nop5p, in complex with fibrillarin from Archaeoglobus fulgidus (AF) and the methyl donor S -adenosyl- L -methionine. The N-terminal domain of Nop5p forms a complementary surface to fibrillarin that serves to anchor the catalytic subunit and to stabilize cofactor binding. A coiled coil in Nop5p mediates dimerization of two fibrillarin–Nop5p heterodimers for optimal interactions with bipartite box C/D RNAs. Structural analysis and complementary biochemical data demonstrate that the conserved C-terminal domain of Nop5p harbors RNA-binding sites. A model of box C/D snoRNP assembly is proposed based on the presented structural and biochemical data.</description><identifier>ISSN: 1545-9993</identifier><identifier>ISSN: 1072-8368</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/nsb905</identifier><identifier>PMID: 12598892</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>Amino Acid Sequence ; Archaeal Proteins - chemistry ; Archaeal Proteins - genetics ; Archaeal Proteins - metabolism ; Archaeoglobus fulgidus - genetics ; Archaeoglobus fulgidus - metabolism ; BASIC BIOLOGICAL SCIENCES ; Binding Sites ; Biochemistry ; BIOLOGICAL FUNCTIONS ; Biological Microscopy ; Biomedical and Life Sciences ; Catalysis ; Chromosomal Proteins, Non-Histone - chemistry ; Chromosomal Proteins, Non-Histone - metabolism ; Crystallography, X-Ray ; Dimerization ; Electrophoretic Mobility Shift Assay ; Life Sciences ; Macromolecular Substances ; Membrane Biology ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; NATIONAL SYNCHROTRON LIGHT SOURCE ; Nuclear Proteins ; PROTEIN STRUCTURE ; Protein Structure, Tertiary ; PROTEINS ; Ribonucleoproteins, Small Nucleolar - chemistry ; Ribonucleoproteins, Small Nucleolar - genetics ; Ribonucleoproteins, Small Nucleolar - metabolism ; RNA Editing ; RNA, Archaeal - chemistry ; RNA, Archaeal - genetics ; RNA, Archaeal - metabolism ; RNA, Guide - chemistry ; RNA, Guide - genetics ; RNA, Guide - metabolism ; RNA, Small Nucleolar - chemistry ; RNA, Small Nucleolar - genetics ; RNA, Small Nucleolar - metabolism ; Sequence Homology, Amino Acid ; Static Electricity ; Structural analysis</subject><ispartof>Nature Structural Biology, 2003-04, Vol.10 (4), p.256-263</ispartof><rights>Springer Nature America, Inc. 2003</rights><rights>Copyright Nature Publishing Group Apr 2003</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c459t-a8787108973bce4fc8e7ed05b0cdc89a18cf365ab17cf3b0c058796ba661c89c3</citedby><cites>FETCH-LOGICAL-c459t-a8787108973bce4fc8e7ed05b0cdc89a18cf365ab17cf3b0c058796ba661c89c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/nsb905$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/nsb905$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,777,781,882,27905,27906,41469,42538,51300</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12598892$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/15008714$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Aittaleb, Mohamed</creatorcontrib><creatorcontrib>Rashid, Rumana</creatorcontrib><creatorcontrib>Chen, Qiong</creatorcontrib><creatorcontrib>Palmer, John R.</creatorcontrib><creatorcontrib>Daniels, Charles J.</creatorcontrib><creatorcontrib>Li, Hong</creatorcontrib><creatorcontrib>Brookhaven National Laboratory, National Synchrotron Light Source (US)</creatorcontrib><title>Structure and function of archaeal box C/D sRNP core proteins</title><title>Nature Structural Biology</title><addtitle>Nat Struct Mol Biol</addtitle><addtitle>Nat Struct Biol</addtitle><description>Nop56p and Nop58p are two core proteins of the box C/D snoRNPs that interact concurrently with fibrillarin and snoRNAs to function in enzyme assembly and catalysis. Here we report the 2.9 Å resolution co-crystal structure of an archaeal homolog of Nop56p/Nop58p, Nop5p, in complex with fibrillarin from Archaeoglobus fulgidus (AF) and the methyl donor S -adenosyl- L -methionine. The N-terminal domain of Nop5p forms a complementary surface to fibrillarin that serves to anchor the catalytic subunit and to stabilize cofactor binding. A coiled coil in Nop5p mediates dimerization of two fibrillarin–Nop5p heterodimers for optimal interactions with bipartite box C/D RNAs. Structural analysis and complementary biochemical data demonstrate that the conserved C-terminal domain of Nop5p harbors RNA-binding sites. A model of box C/D snoRNP assembly is proposed based on the presented structural and biochemical data.</description><subject>Amino Acid Sequence</subject><subject>Archaeal Proteins - chemistry</subject><subject>Archaeal Proteins - genetics</subject><subject>Archaeal Proteins - metabolism</subject><subject>Archaeoglobus fulgidus - genetics</subject><subject>Archaeoglobus fulgidus - metabolism</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>BIOLOGICAL FUNCTIONS</subject><subject>Biological Microscopy</subject><subject>Biomedical and Life Sciences</subject><subject>Catalysis</subject><subject>Chromosomal Proteins, Non-Histone - chemistry</subject><subject>Chromosomal Proteins, Non-Histone - metabolism</subject><subject>Crystallography, X-Ray</subject><subject>Dimerization</subject><subject>Electrophoretic Mobility Shift Assay</subject><subject>Life Sciences</subject><subject>Macromolecular Substances</subject><subject>Membrane Biology</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Molecular Structure</subject><subject>NATIONAL SYNCHROTRON LIGHT SOURCE</subject><subject>Nuclear Proteins</subject><subject>PROTEIN STRUCTURE</subject><subject>Protein Structure, Tertiary</subject><subject>PROTEINS</subject><subject>Ribonucleoproteins, Small Nucleolar - chemistry</subject><subject>Ribonucleoproteins, Small Nucleolar - genetics</subject><subject>Ribonucleoproteins, Small Nucleolar - metabolism</subject><subject>RNA Editing</subject><subject>RNA, Archaeal - chemistry</subject><subject>RNA, Archaeal - genetics</subject><subject>RNA, Archaeal - metabolism</subject><subject>RNA, Guide - chemistry</subject><subject>RNA, Guide - genetics</subject><subject>RNA, Guide - metabolism</subject><subject>RNA, Small Nucleolar - chemistry</subject><subject>RNA, Small Nucleolar - genetics</subject><subject>RNA, Small Nucleolar - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Static Electricity</subject><subject>Structural analysis</subject><issn>1545-9993</issn><issn>1072-8368</issn><issn>1545-9985</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkV1LwzAUhoMoTqf-BCkKelWXtE2TXHgh8xOGih_XIT1LXUeXzCQF_fdGOhzsxqscch6enJMXoSOCLwjO-cj4SmC6hfYILWgqBKfbf7XIB2jf-znGGaUs30UDklHBucj20OVrcB2EzulEmWlSdwZCY01i60Q5mCmt2qSyX8l4dJ34l8fnBGxEl84G3Rh_gHZq1Xp9uDqH6P325m18n06e7h7GV5MUCipCqjjjjGAuWF6BLmrgmukpphWGKXChCIc6L6mqCItFvMWUM1FWqixJ7EM-RKe91_rQSA9N0DADa4yGIAnFOOqLSJ31VBzvs9M-yEXjQbetMtp2XrKcFJiw7F-QcI5zEv9tiE42wLntnImryizjmSg4Kdc2cNZ7p2u5dM1CuW9JsPwNR_bhRPB4ZeuqhZ6usVUaETjvAR9b5kO79XMbqh9wU5Rw</recordid><startdate>20030401</startdate><enddate>20030401</enddate><creator>Aittaleb, Mohamed</creator><creator>Rashid, Rumana</creator><creator>Chen, Qiong</creator><creator>Palmer, John R.</creator><creator>Daniels, Charles J.</creator><creator>Li, Hong</creator><general>Nature Publishing Group US</general><general>Nature Publishing Group</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PADUT</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>20030401</creationdate><title>Structure and function of archaeal box C/D sRNP core proteins</title><author>Aittaleb, Mohamed ; Rashid, Rumana ; Chen, Qiong ; Palmer, John R. ; Daniels, Charles J. ; Li, Hong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c459t-a8787108973bce4fc8e7ed05b0cdc89a18cf365ab17cf3b0c058796ba661c89c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Amino Acid Sequence</topic><topic>Archaeal Proteins - chemistry</topic><topic>Archaeal Proteins - genetics</topic><topic>Archaeal Proteins - metabolism</topic><topic>Archaeoglobus fulgidus - genetics</topic><topic>Archaeoglobus fulgidus - metabolism</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>Binding Sites</topic><topic>Biochemistry</topic><topic>BIOLOGICAL FUNCTIONS</topic><topic>Biological Microscopy</topic><topic>Biomedical and Life Sciences</topic><topic>Catalysis</topic><topic>Chromosomal Proteins, Non-Histone - chemistry</topic><topic>Chromosomal Proteins, Non-Histone - metabolism</topic><topic>Crystallography, X-Ray</topic><topic>Dimerization</topic><topic>Electrophoretic Mobility Shift Assay</topic><topic>Life Sciences</topic><topic>Macromolecular Substances</topic><topic>Membrane Biology</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Molecular Structure</topic><topic>NATIONAL SYNCHROTRON LIGHT SOURCE</topic><topic>Nuclear Proteins</topic><topic>PROTEIN STRUCTURE</topic><topic>Protein Structure, Tertiary</topic><topic>PROTEINS</topic><topic>Ribonucleoproteins, Small Nucleolar - chemistry</topic><topic>Ribonucleoproteins, Small Nucleolar - genetics</topic><topic>Ribonucleoproteins, Small Nucleolar - metabolism</topic><topic>RNA Editing</topic><topic>RNA, Archaeal - chemistry</topic><topic>RNA, Archaeal - genetics</topic><topic>RNA, Archaeal - metabolism</topic><topic>RNA, Guide - chemistry</topic><topic>RNA, Guide - genetics</topic><topic>RNA, Guide - metabolism</topic><topic>RNA, Small Nucleolar - chemistry</topic><topic>RNA, Small Nucleolar - genetics</topic><topic>RNA, Small Nucleolar - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Static Electricity</topic><topic>Structural analysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Aittaleb, Mohamed</creatorcontrib><creatorcontrib>Rashid, Rumana</creatorcontrib><creatorcontrib>Chen, Qiong</creatorcontrib><creatorcontrib>Palmer, John R.</creatorcontrib><creatorcontrib>Daniels, Charles J.</creatorcontrib><creatorcontrib>Li, Hong</creatorcontrib><creatorcontrib>Brookhaven National Laboratory, National Synchrotron Light Source (US)</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium &amp; Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health &amp; Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Research Library China</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Nature Structural Biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Aittaleb, Mohamed</au><au>Rashid, Rumana</au><au>Chen, Qiong</au><au>Palmer, John R.</au><au>Daniels, Charles J.</au><au>Li, Hong</au><aucorp>Brookhaven National Laboratory, National Synchrotron Light Source (US)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure and function of archaeal box C/D sRNP core proteins</atitle><jtitle>Nature Structural Biology</jtitle><stitle>Nat Struct Mol Biol</stitle><addtitle>Nat Struct Biol</addtitle><date>2003-04-01</date><risdate>2003</risdate><volume>10</volume><issue>4</issue><spage>256</spage><epage>263</epage><pages>256-263</pages><issn>1545-9993</issn><issn>1072-8368</issn><eissn>1545-9985</eissn><abstract>Nop56p and Nop58p are two core proteins of the box C/D snoRNPs that interact concurrently with fibrillarin and snoRNAs to function in enzyme assembly and catalysis. Here we report the 2.9 Å resolution co-crystal structure of an archaeal homolog of Nop56p/Nop58p, Nop5p, in complex with fibrillarin from Archaeoglobus fulgidus (AF) and the methyl donor S -adenosyl- L -methionine. The N-terminal domain of Nop5p forms a complementary surface to fibrillarin that serves to anchor the catalytic subunit and to stabilize cofactor binding. A coiled coil in Nop5p mediates dimerization of two fibrillarin–Nop5p heterodimers for optimal interactions with bipartite box C/D RNAs. Structural analysis and complementary biochemical data demonstrate that the conserved C-terminal domain of Nop5p harbors RNA-binding sites. A model of box C/D snoRNP assembly is proposed based on the presented structural and biochemical data.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>12598892</pmid><doi>10.1038/nsb905</doi><tpages>8</tpages></addata></record>
fulltext fulltext
identifier ISSN: 1545-9993
ispartof Nature Structural Biology, 2003-04, Vol.10 (4), p.256-263
issn 1545-9993
1072-8368
1545-9985
language eng
recordid cdi_proquest_miscellaneous_73140172
source MEDLINE; Nature; Springer Nature - Complete Springer Journals
subjects Amino Acid Sequence
Archaeal Proteins - chemistry
Archaeal Proteins - genetics
Archaeal Proteins - metabolism
Archaeoglobus fulgidus - genetics
Archaeoglobus fulgidus - metabolism
BASIC BIOLOGICAL SCIENCES
Binding Sites
Biochemistry
BIOLOGICAL FUNCTIONS
Biological Microscopy
Biomedical and Life Sciences
Catalysis
Chromosomal Proteins, Non-Histone - chemistry
Chromosomal Proteins, Non-Histone - metabolism
Crystallography, X-Ray
Dimerization
Electrophoretic Mobility Shift Assay
Life Sciences
Macromolecular Substances
Membrane Biology
Models, Molecular
Molecular Sequence Data
Molecular Structure
NATIONAL SYNCHROTRON LIGHT SOURCE
Nuclear Proteins
PROTEIN STRUCTURE
Protein Structure, Tertiary
PROTEINS
Ribonucleoproteins, Small Nucleolar - chemistry
Ribonucleoproteins, Small Nucleolar - genetics
Ribonucleoproteins, Small Nucleolar - metabolism
RNA Editing
RNA, Archaeal - chemistry
RNA, Archaeal - genetics
RNA, Archaeal - metabolism
RNA, Guide - chemistry
RNA, Guide - genetics
RNA, Guide - metabolism
RNA, Small Nucleolar - chemistry
RNA, Small Nucleolar - genetics
RNA, Small Nucleolar - metabolism
Sequence Homology, Amino Acid
Static Electricity
Structural analysis
title Structure and function of archaeal box C/D sRNP core proteins
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-20T15%3A59%3A37IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_osti_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Structure%20and%20function%20of%20archaeal%20box%20C/D%20sRNP%20core%20proteins&rft.jtitle=Nature%20Structural%20Biology&rft.au=Aittaleb,%20Mohamed&rft.aucorp=Brookhaven%20National%20Laboratory,%20National%20Synchrotron%20Light%20Source%20(US)&rft.date=2003-04-01&rft.volume=10&rft.issue=4&rft.spage=256&rft.epage=263&rft.pages=256-263&rft.issn=1545-9993&rft.eissn=1545-9985&rft_id=info:doi/10.1038/nsb905&rft_dat=%3Cproquest_osti_%3E73140172%3C/proquest_osti_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=228294816&rft_id=info:pmid/12598892&rfr_iscdi=true