Structure of a membrane-based steric chaperone in complex with its lipase substrate
Secretion via the type II secretion pathway in Gram-negative bacteria often relies crucially on steric chaperones in the periplasm. Here, we report the crystal structure of the soluble form of a lipase-specific foldase (Lif) from Burkholderia glumae in complex with its cognate lipase. The structure...
Gespeichert in:
Veröffentlicht in: | Nature structural & molecular biology 2006-04, Vol.13 (4), p.374-375 |
---|---|
Hauptverfasser: | , , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 375 |
---|---|
container_issue | 4 |
container_start_page | 374 |
container_title | Nature structural & molecular biology |
container_volume | 13 |
creator | Pauwels, Kris Lustig, Ariel Wyns, Lode Tommassen, Jan Savvides, Savvas N Van Gelder, Patrick |
description | Secretion via the type II secretion pathway in Gram-negative bacteria often relies crucially on steric chaperones in the periplasm. Here, we report the crystal structure of the soluble form of a lipase-specific foldase (Lif) from
Burkholderia glumae
in complex with its cognate lipase. The structure reveals how Lif uses a novel α-helical scaffold to embrace lipase, thereby creating an unusually extensive folding platform. |
doi_str_mv | 10.1038/nsmb1065 |
format | Article |
fullrecord | <record><control><sourceid>gale_proqu</sourceid><recordid>TN_cdi_proquest_miscellaneous_67987621</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A185380051</galeid><sourcerecordid>A185380051</sourcerecordid><originalsourceid>FETCH-LOGICAL-c474t-77bda7895c744dbe4bfa7d93adc5000fc904b0d7fe60d12aa0f0a5f4108cc0323</originalsourceid><addsrcrecordid>eNqFkl1rFDEUhgdRbK2Cv0CCgtiLqSeTySS5LMWPQqHg6nXIZE62KfNlkqH135tlV5etQslFwslz3pM3vEXxmsIZBSY_jnFoKTT8SXFMec1LpSR_-ves2FHxIsZbgIpzwZ4XR7ThVDKljovVKoXFpiUgmRwxZMChDWbEsjUROxITBm-JvTEzhmlE4kdip2Hu8Z7c-XRDfIqk93OGSVzamIJJ-LJ45kwf8dVuPyl-fP70_eJreXX95fLi_Kq0tahTKUTbGSEVt6Kuuxbr1hnRKWY6ywHAWQV1C51w2EBHK2PAgeGupiCtBVaxk-L9VncO088FY9KDjxb7Pr9_WqJuhJKiqeijIBVUCl5BBt8-AG-nJYzZhK4qyYAKVmfo3RZamx61H92UXduNoj6nkjMJwDczz_5D5dXh4G3-Sudz_aDh9KAhMwnv09osMerL1bdD9sOWtWGKMaDTc_CDCb80Bb1JhP6TiIy-2Vla2gG7PbiLwH5uzFfjGsPe8z9ivwEl2LzF</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>228301734</pqid></control><display><type>article</type><title>Structure of a membrane-based steric chaperone in complex with its lipase substrate</title><source>MEDLINE</source><source>Nature Journals Online</source><source>SpringerLink Journals - AutoHoldings</source><creator>Pauwels, Kris ; Lustig, Ariel ; Wyns, Lode ; Tommassen, Jan ; Savvides, Savvas N ; Van Gelder, Patrick</creator><creatorcontrib>Pauwels, Kris ; Lustig, Ariel ; Wyns, Lode ; Tommassen, Jan ; Savvides, Savvas N ; Van Gelder, Patrick</creatorcontrib><description>Secretion via the type II secretion pathway in Gram-negative bacteria often relies crucially on steric chaperones in the periplasm. Here, we report the crystal structure of the soluble form of a lipase-specific foldase (Lif) from
Burkholderia glumae
in complex with its cognate lipase. The structure reveals how Lif uses a novel α-helical scaffold to embrace lipase, thereby creating an unusually extensive folding platform.</description><identifier>ISSN: 1545-9993</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/nsmb1065</identifier><identifier>PMID: 16518399</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>Bacteria ; Bacterial Proteins - chemistry ; Bacterial Proteins - metabolism ; Biochemistry ; Biological Microscopy ; Biomedical and Life Sciences ; brief-communication ; Burkholderia - enzymology ; Burkholderia glumae ; Life Sciences ; Lipase ; Lipase - chemistry ; Lipase - metabolism ; Membrane Biology ; Membrane proteins ; Models, Molecular ; Molecular biology ; Molecular Chaperones - chemistry ; Molecular Chaperones - metabolism ; Molecular structure ; Multiprotein Complexes ; Physiological aspects ; Protein Folding ; Protein Structure ; Protein Structure, Secondary ; Structure ; Substrate Specificity</subject><ispartof>Nature structural & molecular biology, 2006-04, Vol.13 (4), p.374-375</ispartof><rights>Springer Nature America, Inc. 2006</rights><rights>COPYRIGHT 2006 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Apr 2006</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c474t-77bda7895c744dbe4bfa7d93adc5000fc904b0d7fe60d12aa0f0a5f4108cc0323</citedby><cites>FETCH-LOGICAL-c474t-77bda7895c744dbe4bfa7d93adc5000fc904b0d7fe60d12aa0f0a5f4108cc0323</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/nsmb1065$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/nsmb1065$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,777,781,27905,27906,41469,42538,51300</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16518399$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pauwels, Kris</creatorcontrib><creatorcontrib>Lustig, Ariel</creatorcontrib><creatorcontrib>Wyns, Lode</creatorcontrib><creatorcontrib>Tommassen, Jan</creatorcontrib><creatorcontrib>Savvides, Savvas N</creatorcontrib><creatorcontrib>Van Gelder, Patrick</creatorcontrib><title>Structure of a membrane-based steric chaperone in complex with its lipase substrate</title><title>Nature structural & molecular biology</title><addtitle>Nat Struct Mol Biol</addtitle><addtitle>Nat Struct Mol Biol</addtitle><description>Secretion via the type II secretion pathway in Gram-negative bacteria often relies crucially on steric chaperones in the periplasm. Here, we report the crystal structure of the soluble form of a lipase-specific foldase (Lif) from
Burkholderia glumae
in complex with its cognate lipase. The structure reveals how Lif uses a novel α-helical scaffold to embrace lipase, thereby creating an unusually extensive folding platform.</description><subject>Bacteria</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biochemistry</subject><subject>Biological Microscopy</subject><subject>Biomedical and Life Sciences</subject><subject>brief-communication</subject><subject>Burkholderia - enzymology</subject><subject>Burkholderia glumae</subject><subject>Life Sciences</subject><subject>Lipase</subject><subject>Lipase - chemistry</subject><subject>Lipase - metabolism</subject><subject>Membrane Biology</subject><subject>Membrane proteins</subject><subject>Models, Molecular</subject><subject>Molecular biology</subject><subject>Molecular Chaperones - chemistry</subject><subject>Molecular Chaperones - metabolism</subject><subject>Molecular structure</subject><subject>Multiprotein Complexes</subject><subject>Physiological aspects</subject><subject>Protein Folding</subject><subject>Protein Structure</subject><subject>Protein Structure, Secondary</subject><subject>Structure</subject><subject>Substrate Specificity</subject><issn>1545-9993</issn><issn>1545-9985</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</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>eNqFkl1rFDEUhgdRbK2Cv0CCgtiLqSeTySS5LMWPQqHg6nXIZE62KfNlkqH135tlV5etQslFwslz3pM3vEXxmsIZBSY_jnFoKTT8SXFMec1LpSR_-ves2FHxIsZbgIpzwZ4XR7ThVDKljovVKoXFpiUgmRwxZMChDWbEsjUROxITBm-JvTEzhmlE4kdip2Hu8Z7c-XRDfIqk93OGSVzamIJJ-LJ45kwf8dVuPyl-fP70_eJreXX95fLi_Kq0tahTKUTbGSEVt6Kuuxbr1hnRKWY6ywHAWQV1C51w2EBHK2PAgeGupiCtBVaxk-L9VncO088FY9KDjxb7Pr9_WqJuhJKiqeijIBVUCl5BBt8-AG-nJYzZhK4qyYAKVmfo3RZamx61H92UXduNoj6nkjMJwDczz_5D5dXh4G3-Sudz_aDh9KAhMwnv09osMerL1bdD9sOWtWGKMaDTc_CDCb80Bb1JhP6TiIy-2Vla2gG7PbiLwH5uzFfjGsPe8z9ivwEl2LzF</recordid><startdate>20060401</startdate><enddate>20060401</enddate><creator>Pauwels, Kris</creator><creator>Lustig, Ariel</creator><creator>Wyns, Lode</creator><creator>Tommassen, Jan</creator><creator>Savvides, Savvas N</creator><creator>Van Gelder, Patrick</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>ISR</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></search><sort><creationdate>20060401</creationdate><title>Structure of a membrane-based steric chaperone in complex with its lipase substrate</title><author>Pauwels, Kris ; Lustig, Ariel ; Wyns, Lode ; Tommassen, Jan ; Savvides, Savvas N ; Van Gelder, Patrick</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c474t-77bda7895c744dbe4bfa7d93adc5000fc904b0d7fe60d12aa0f0a5f4108cc0323</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Bacteria</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - metabolism</topic><topic>Biochemistry</topic><topic>Biological Microscopy</topic><topic>Biomedical and Life Sciences</topic><topic>brief-communication</topic><topic>Burkholderia - enzymology</topic><topic>Burkholderia glumae</topic><topic>Life Sciences</topic><topic>Lipase</topic><topic>Lipase - chemistry</topic><topic>Lipase - metabolism</topic><topic>Membrane Biology</topic><topic>Membrane proteins</topic><topic>Models, Molecular</topic><topic>Molecular biology</topic><topic>Molecular Chaperones - chemistry</topic><topic>Molecular Chaperones - metabolism</topic><topic>Molecular structure</topic><topic>Multiprotein Complexes</topic><topic>Physiological aspects</topic><topic>Protein Folding</topic><topic>Protein Structure</topic><topic>Protein Structure, Secondary</topic><topic>Structure</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pauwels, Kris</creatorcontrib><creatorcontrib>Lustig, Ariel</creatorcontrib><creatorcontrib>Wyns, Lode</creatorcontrib><creatorcontrib>Tommassen, Jan</creatorcontrib><creatorcontrib>Savvides, Savvas N</creatorcontrib><creatorcontrib>Van Gelder, Patrick</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & 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 & 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 & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & 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><jtitle>Nature structural & molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pauwels, Kris</au><au>Lustig, Ariel</au><au>Wyns, Lode</au><au>Tommassen, Jan</au><au>Savvides, Savvas N</au><au>Van Gelder, Patrick</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure of a membrane-based steric chaperone in complex with its lipase substrate</atitle><jtitle>Nature structural & molecular biology</jtitle><stitle>Nat Struct Mol Biol</stitle><addtitle>Nat Struct Mol Biol</addtitle><date>2006-04-01</date><risdate>2006</risdate><volume>13</volume><issue>4</issue><spage>374</spage><epage>375</epage><pages>374-375</pages><issn>1545-9993</issn><eissn>1545-9985</eissn><abstract>Secretion via the type II secretion pathway in Gram-negative bacteria often relies crucially on steric chaperones in the periplasm. Here, we report the crystal structure of the soluble form of a lipase-specific foldase (Lif) from
Burkholderia glumae
in complex with its cognate lipase. The structure reveals how Lif uses a novel α-helical scaffold to embrace lipase, thereby creating an unusually extensive folding platform.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>16518399</pmid><doi>10.1038/nsmb1065</doi><tpages>2</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1545-9993 |
ispartof | Nature structural & molecular biology, 2006-04, Vol.13 (4), p.374-375 |
issn | 1545-9993 1545-9985 |
language | eng |
recordid | cdi_proquest_miscellaneous_67987621 |
source | MEDLINE; Nature Journals Online; SpringerLink Journals - AutoHoldings |
subjects | Bacteria Bacterial Proteins - chemistry Bacterial Proteins - metabolism Biochemistry Biological Microscopy Biomedical and Life Sciences brief-communication Burkholderia - enzymology Burkholderia glumae Life Sciences Lipase Lipase - chemistry Lipase - metabolism Membrane Biology Membrane proteins Models, Molecular Molecular biology Molecular Chaperones - chemistry Molecular Chaperones - metabolism Molecular structure Multiprotein Complexes Physiological aspects Protein Folding Protein Structure Protein Structure, Secondary Structure Substrate Specificity |
title | Structure of a membrane-based steric chaperone in complex with its lipase substrate |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-19T05%3A27%3A02IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Structure%20of%20a%20membrane-based%20steric%20chaperone%20in%20complex%20with%20its%20lipase%20substrate&rft.jtitle=Nature%20structural%20&%20molecular%20biology&rft.au=Pauwels,%20Kris&rft.date=2006-04-01&rft.volume=13&rft.issue=4&rft.spage=374&rft.epage=375&rft.pages=374-375&rft.issn=1545-9993&rft.eissn=1545-9985&rft_id=info:doi/10.1038/nsmb1065&rft_dat=%3Cgale_proqu%3EA185380051%3C/gale_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=228301734&rft_id=info:pmid/16518399&rft_galeid=A185380051&rfr_iscdi=true |