1ici
From Proteopedia
(Difference between revisions)
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<StructureSection load='1ici' size='340' side='right'caption='[[1ici]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1ici' size='340' side='right'caption='[[1ici]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1ici]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1ici]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ICI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ICI FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ici FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ici OCA], [https://pdbe.org/1ici PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ici RCSB], [https://www.ebi.ac.uk/pdbsum/1ici PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ici ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/NPD1_ARCFU NPD1_ARCFU] NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Deacetylates the N-terminal lysine residue of Alba, the major archaeal chromatin protein and that, in turn, increases Alba's DNA binding affinity, thereby repressing transcription (By similarity).<ref>PMID:10841563</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ici ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ici ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | 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 A and 2.4 A 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. | ||
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- | Crystal structure of a SIR2 homolog-NAD complex.,Min J, Landry J, Sternglanz R, Xu RM Cell. 2001 Apr 20;105(2):269-79. PMID:11336676<ref>PMID:11336676</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1ici" style="background-color:#fffaf0;"></div> | ||
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- | ==See Also== | ||
- | *[[Journal:JBSD:28|Journal:JBSD:28]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Archaeoglobus fulgidus]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Landry | + | [[Category: Landry J]] |
- | [[Category: Min | + | [[Category: Min J]] |
- | [[Category: Sternglanz | + | [[Category: Sternglanz R]] |
- | [[Category: Xu | + | [[Category: Xu R-M]] |
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Current revision
CRYSTAL STRUCTURE OF A SIR2 HOMOLOG-NAD COMPLEX
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