Crystal Structure of a SIR2 Homolog–NAD Complex
The SIR2 protein family comprises a novel class of nicotinamide-adenine dinucleotide (NAD)-dependent protein deacetylases that function in transcriptional silencing, DNA repair, and life-span extension in Saccharomyces cerevisiae. Two crystal structures of a SIR2 homolog from Archaeoglobus fulgidus...
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| Veröffentlicht in: | Cell 2001-04, Vol.105 (2), p.269-279 |
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| creator | Min, Jinrong Landry, Joseph Sternglanz, Rolf Xu, Rui-Ming |
| description | The SIR2 protein family comprises a novel class of nicotinamide-adenine dinucleotide (NAD)-dependent protein deacetylases that function in transcriptional silencing, DNA repair, and life-span extension in
Saccharomyces cerevisiae. Two crystal structures of a SIR2 homolog from
Archaeoglobus fulgidus complexed with NAD have been determined at 2.1 Å and 2.4 Å resolutions. The structures reveal that the protein consists of a large domain having a Rossmann fold and a small domain containing a three-stranded zinc ribbon motif. NAD is bound in a pocket between the two domains. A distinct mode of NAD binding and an unusual configuration of the zinc ribbon motif are observed. The structures also provide important insights into the catalytic mechanism of NAD-dependent protein deacetylation by this family of enzymes. |
| doi_str_mv | 10.1016/S0092-8674(01)00317-8 |
| format | Article |
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Saccharomyces cerevisiae. Two crystal structures of a SIR2 homolog from
Archaeoglobus fulgidus complexed with NAD have been determined at 2.1 Å and 2.4 Å resolutions. The structures reveal that the protein consists of a large domain having a Rossmann fold and a small domain containing a three-stranded zinc ribbon motif. NAD is bound in a pocket between the two domains. A distinct mode of NAD binding and an unusual configuration of the zinc ribbon motif are observed. The structures also provide important insights into the catalytic mechanism of NAD-dependent protein deacetylation by this family of enzymes.</description><identifier>ISSN: 0092-8674</identifier><identifier>EISSN: 1097-4172</identifier><identifier>DOI: 10.1016/S0092-8674(01)00317-8</identifier><identifier>PMID: 11336676</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Archaeal Proteins - chemistry ; Archaeal Proteins - genetics ; Archaeal Proteins - metabolism ; Archaeoglobus fulgidus - chemistry ; Archaeoglobus fulgidus - genetics ; Binding Sites ; COMPLEXES ; CRYSTAL STRUCTURE ; Crystallography, X-Ray ; Histone Deacetylases - chemistry ; Histone Deacetylases - genetics ; Histone Deacetylases - metabolism ; MATERIALS SCIENCE ; Models, Molecular ; Molecular Sequence Data ; NAD - chemistry ; NAD - metabolism ; NATIONAL SYNCHROTRON LIGHT SOURCE ; NSLS ; Protein Structure, Tertiary ; Sequence Alignment ; Silent Information Regulator Proteins, Saccharomyces cerevisiae ; Sirtuin 2 ; Sirtuins ; Trans-Activators - chemistry ; Trans-Activators - genetics ; Trans-Activators - metabolism</subject><ispartof>Cell, 2001-04, Vol.105 (2), p.269-279</ispartof><rights>2001 Cell Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c500t-add77618d405227720cac0dd0f05191dc9dfec1510c2a7561aa994f12e5ed4843</citedby><cites>FETCH-LOGICAL-c500t-add77618d405227720cac0dd0f05191dc9dfec1510c2a7561aa994f12e5ed4843</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0092-8674(01)00317-8$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,780,784,885,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11336676$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/796381$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Min, Jinrong</creatorcontrib><creatorcontrib>Landry, Joseph</creatorcontrib><creatorcontrib>Sternglanz, Rolf</creatorcontrib><creatorcontrib>Xu, Rui-Ming</creatorcontrib><creatorcontrib>Brookhaven National Lab., Upton, NY (US)</creatorcontrib><creatorcontrib>National Synchrotron Light Source (US)</creatorcontrib><title>Crystal Structure of a SIR2 Homolog–NAD Complex</title><title>Cell</title><addtitle>Cell</addtitle><description>The SIR2 protein family comprises a novel class of nicotinamide-adenine dinucleotide (NAD)-dependent protein deacetylases that function in transcriptional silencing, DNA repair, and life-span extension in
Saccharomyces cerevisiae. Two crystal structures of a SIR2 homolog from
Archaeoglobus fulgidus complexed with NAD have been determined at 2.1 Å and 2.4 Å resolutions. The structures reveal that the protein consists of a large domain having a Rossmann fold and a small domain containing a three-stranded zinc ribbon motif. NAD is bound in a pocket between the two domains. A distinct mode of NAD binding and an unusual configuration of the zinc ribbon motif are observed. The structures also provide important insights into the catalytic mechanism of NAD-dependent protein deacetylation by this family of enzymes.</description><subject>Amino Acid Sequence</subject><subject>Archaeal Proteins - chemistry</subject><subject>Archaeal Proteins - genetics</subject><subject>Archaeal Proteins - metabolism</subject><subject>Archaeoglobus fulgidus - chemistry</subject><subject>Archaeoglobus fulgidus - genetics</subject><subject>Binding Sites</subject><subject>COMPLEXES</subject><subject>CRYSTAL STRUCTURE</subject><subject>Crystallography, X-Ray</subject><subject>Histone Deacetylases - chemistry</subject><subject>Histone Deacetylases - genetics</subject><subject>Histone Deacetylases - metabolism</subject><subject>MATERIALS SCIENCE</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>NAD - chemistry</subject><subject>NAD - metabolism</subject><subject>NATIONAL SYNCHROTRON LIGHT SOURCE</subject><subject>NSLS</subject><subject>Protein Structure, Tertiary</subject><subject>Sequence Alignment</subject><subject>Silent Information Regulator Proteins, Saccharomyces cerevisiae</subject><subject>Sirtuin 2</subject><subject>Sirtuins</subject><subject>Trans-Activators - chemistry</subject><subject>Trans-Activators - genetics</subject><subject>Trans-Activators - metabolism</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMtOwzAQRS0EgvL4BFDYIFgEZpw4TlaoKk8JgURhbRl7AkFJXewEwY5_4A_5EhpawZLVbM6de3UY20Y4RMDsaAxQ8DjPZLoPeACQoIzzJTZAKGScouTLbPCLrLH1EJ4BIBdCrLI1xCTJMpkNGI78e2h1HY1b35m28xS5MtLR-PKWRxeucbV7_Pr4vB6eRCPXTGt622Qrpa4DbS3uBrs_O70bXcRXN-eXo-FVbARAG2trpcwwtykIzqXkYLQBa6EEgQVaU9iSDAoEw7UUGWpdFGmJnATZNE-TDbY7_-tCW6lgqpbMk3GTCZlWySJLcpwxe3Nm6t1LR6FVTRUM1bWekOuCkpBzkfIeFHPQeBeCp1JNfdVo_64QVO9T_fhUvSwFqH58qnyW21kUdA8N2b_UQuAMOJ4DNFPxWpHvl9LEkK18P9S66p-Kb-vLgug</recordid><startdate>20010420</startdate><enddate>20010420</enddate><creator>Min, Jinrong</creator><creator>Landry, Joseph</creator><creator>Sternglanz, Rolf</creator><creator>Xu, Rui-Ming</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><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>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>20010420</creationdate><title>Crystal Structure of a SIR2 Homolog–NAD Complex</title><author>Min, Jinrong ; Landry, Joseph ; Sternglanz, Rolf ; Xu, Rui-Ming</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c500t-add77618d405227720cac0dd0f05191dc9dfec1510c2a7561aa994f12e5ed4843</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Amino Acid Sequence</topic><topic>Archaeal Proteins - chemistry</topic><topic>Archaeal Proteins - genetics</topic><topic>Archaeal Proteins - metabolism</topic><topic>Archaeoglobus fulgidus - chemistry</topic><topic>Archaeoglobus fulgidus - genetics</topic><topic>Binding Sites</topic><topic>COMPLEXES</topic><topic>CRYSTAL STRUCTURE</topic><topic>Crystallography, X-Ray</topic><topic>Histone Deacetylases - chemistry</topic><topic>Histone Deacetylases - genetics</topic><topic>Histone Deacetylases - metabolism</topic><topic>MATERIALS SCIENCE</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>NAD - chemistry</topic><topic>NAD - metabolism</topic><topic>NATIONAL SYNCHROTRON LIGHT SOURCE</topic><topic>NSLS</topic><topic>Protein Structure, Tertiary</topic><topic>Sequence Alignment</topic><topic>Silent Information Regulator Proteins, Saccharomyces cerevisiae</topic><topic>Sirtuin 2</topic><topic>Sirtuins</topic><topic>Trans-Activators - chemistry</topic><topic>Trans-Activators - genetics</topic><topic>Trans-Activators - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Min, Jinrong</creatorcontrib><creatorcontrib>Landry, Joseph</creatorcontrib><creatorcontrib>Sternglanz, Rolf</creatorcontrib><creatorcontrib>Xu, Rui-Ming</creatorcontrib><creatorcontrib>Brookhaven National Lab., Upton, NY (US)</creatorcontrib><creatorcontrib>National Synchrotron Light Source (US)</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Min, Jinrong</au><au>Landry, Joseph</au><au>Sternglanz, Rolf</au><au>Xu, Rui-Ming</au><aucorp>Brookhaven National Lab., Upton, NY (US)</aucorp><aucorp>National Synchrotron Light Source (US)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal Structure of a SIR2 Homolog–NAD Complex</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>2001-04-20</date><risdate>2001</risdate><volume>105</volume><issue>2</issue><spage>269</spage><epage>279</epage><pages>269-279</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><abstract>The SIR2 protein family comprises a novel class of nicotinamide-adenine dinucleotide (NAD)-dependent protein deacetylases that function in transcriptional silencing, DNA repair, and life-span extension in
Saccharomyces cerevisiae. Two crystal structures of a SIR2 homolog from
Archaeoglobus fulgidus complexed with NAD have been determined at 2.1 Å and 2.4 Å resolutions. The structures reveal that the protein consists of a large domain having a Rossmann fold and a small domain containing a three-stranded zinc ribbon motif. NAD is bound in a pocket between the two domains. A distinct mode of NAD binding and an unusual configuration of the zinc ribbon motif are observed. The structures also provide important insights into the catalytic mechanism of NAD-dependent protein deacetylation by this family of enzymes.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>11336676</pmid><doi>10.1016/S0092-8674(01)00317-8</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Cell Press Free Archives; Access via ScienceDirect (Elsevier); EZB-FREE-00999 freely available EZB journals |
| subjects | Amino Acid Sequence Archaeal Proteins - chemistry Archaeal Proteins - genetics Archaeal Proteins - metabolism Archaeoglobus fulgidus - chemistry Archaeoglobus fulgidus - genetics Binding Sites COMPLEXES CRYSTAL STRUCTURE Crystallography, X-Ray Histone Deacetylases - chemistry Histone Deacetylases - genetics Histone Deacetylases - metabolism MATERIALS SCIENCE Models, Molecular Molecular Sequence Data NAD - chemistry NAD - metabolism NATIONAL SYNCHROTRON LIGHT SOURCE NSLS Protein Structure, Tertiary Sequence Alignment Silent Information Regulator Proteins, Saccharomyces cerevisiae Sirtuin 2 Sirtuins Trans-Activators - chemistry Trans-Activators - genetics Trans-Activators - metabolism |
| title | Crystal Structure of a SIR2 Homolog–NAD Complex |
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