2od7

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[[Image:2od7.gif|left|200px]]<br /><applet load="2od7" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2od7.gif|left|200px]]
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caption="2od7, resolution 2.000&Aring;" />
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'''Crystal Structure of yHst2 bound to the intermediate analogue ADP-HPD, and and aceylated H4 peptide'''<br />
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{{Structure
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|PDB= 2od7 |SIZE=350|CAPTION= <scene name='initialview01'>2od7</scene>, resolution 2.000&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=A1R:5'-O-[(S)-{[(S)-{[(2R,3R,4S)-3,4-DIHYDROXYPYRROLIDIN-2-YL]METHOXY}(HYDROXY)PHOSPHORYL]OXY}(HYDROXY)PHOSPHORYL]ADENOSINE'>A1R</scene>
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|ACTIVITY=
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|GENE= HST2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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}}
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'''Crystal Structure of yHst2 bound to the intermediate analogue ADP-HPD, and and aceylated H4 peptide'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2OD7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=A1R:'>A1R</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OD7 OCA].
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2OD7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OD7 OCA].
==Reference==
==Reference==
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Structural basis for nicotinamide inhibition and base exchange in Sir2 enzymes., Sanders BD, Zhao K, Slama JT, Marmorstein R, Mol Cell. 2007 Feb 9;25(3):463-72. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17289592 17289592]
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Structural basis for nicotinamide inhibition and base exchange in Sir2 enzymes., Sanders BD, Zhao K, Slama JT, Marmorstein R, Mol Cell. 2007 Feb 9;25(3):463-72. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17289592 17289592]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: zn binding domain]]
[[Category: zn binding domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:17:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:58:09 2008''

Revision as of 15:58, 20 March 2008


PDB ID 2od7

Drag the structure with the mouse to rotate
, resolution 2.000Å
Ligands: and
Gene: HST2 (Saccharomyces cerevisiae)
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of yHst2 bound to the intermediate analogue ADP-HPD, and and aceylated H4 peptide


Overview

The Sir2 family of proteins consists of broadly conserved NAD(+)-dependent deacetylases that are implicated in diverse biological processes, including DNA regulation, metabolism, and longevity. Sir2 proteins are regulated in part by the cellular concentrations of a noncompetitive inhibitor, nicotinamide, that reacts with a Sir2 reaction intermediate via a base-exchange reaction to reform NAD(+) at the expense of deacetylation. To gain a mechanistic understanding of nicotinamide inhibition in Sir2 enzymes, we captured the structure of nicotinamide bound to a Sir2 homolog, yeast Hst2, in complex with its acetyl-lysine 16 histone H4 substrate and a reaction intermediate analog, ADP-HPD. Together with related biochemical studies and structures, we identify a nicotinamide inhibition and base-exchange site that is distinct from the so-called "C pocket" binding site for the nicotinamide group of NAD(+). These results provide insights into the Sir2 mechanism of nicotinamide inhibition and have important implications for the development of Sir2-specific effectors.

About this Structure

2OD7 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Structural basis for nicotinamide inhibition and base exchange in Sir2 enzymes., Sanders BD, Zhao K, Slama JT, Marmorstein R, Mol Cell. 2007 Feb 9;25(3):463-72. PMID:17289592

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