1ici

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(New page: 200px<br /><applet load="1ici" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ici, resolution 2.1&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1ici.gif|left|200px]]<br /><applet load="1ici" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ici, resolution 2.1&Aring;" />
 
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'''CRYSTAL STRUCTURE OF A SIR2 HOMOLOG-NAD COMPLEX'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF A SIR2 HOMOLOG-NAD COMPLEX==
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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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<StructureSection load='1ici' size='340' side='right'caption='[[1ici]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<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>
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1ICI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] with ZN and NAD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ICI OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<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>
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==Reference==
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<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>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11336676 11336676]
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ic/1ici_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Archaeoglobus fulgidus]]
[[Category: Archaeoglobus fulgidus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Landry, J.]]
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[[Category: Landry J]]
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[[Category: Min, J.]]
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[[Category: Min J]]
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[[Category: Sternglanz, R.]]
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[[Category: Sternglanz R]]
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[[Category: Xu, R.M.]]
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[[Category: Xu R-M]]
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[[Category: NAD]]
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[[Category: ZN]]
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[[Category: nad-binding]]
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[[Category: protein deacetylase]]
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[[Category: rossmann fold]]
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[[Category: zinc ribbon]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:16:55 2007''
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Current revision

CRYSTAL STRUCTURE OF A SIR2 HOMOLOG-NAD COMPLEX

PDB ID 1ici

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