1ici
From Proteopedia
(New page: 200px<br /><applet load="1ici" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ici, resolution 2.1Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1ici.gif|left|200px]]<br /><applet load="1ici" size=" | + | [[Image:1ici.gif|left|200px]]<br /><applet load="1ici" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ici, resolution 2.1Å" /> | caption="1ici, resolution 2.1Å" /> | ||
'''CRYSTAL STRUCTURE OF A SIR2 HOMOLOG-NAD COMPLEX'''<br /> | '''CRYSTAL STRUCTURE OF A SIR2 HOMOLOG-NAD COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The SIR2 protein family comprises a novel class of nicotinamide-adenine | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 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:// | + | 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 <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ICI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Min, J.]] | [[Category: Min, J.]] | ||
[[Category: Sternglanz, R.]] | [[Category: Sternglanz, R.]] | ||
| - | [[Category: Xu, R | + | [[Category: Xu, R M.]] |
[[Category: NAD]] | [[Category: NAD]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
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[[Category: zinc ribbon]] | [[Category: zinc ribbon]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:10:21 2008'' |
Revision as of 11:10, 21 February 2008
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CRYSTAL STRUCTURE OF A SIR2 HOMOLOG-NAD COMPLEX
Overview
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.
About this Structure
1ICI is a Single protein structure of sequence from Archaeoglobus fulgidus with and as ligands. Full crystallographic information is available from OCA.
Reference
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
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