2qqf

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|PDB= 2qqf |SIZE=350|CAPTION= <scene name='initialview01'>2qqf</scene>, resolution 2.0&Aring;
|PDB= 2qqf |SIZE=350|CAPTION= <scene name='initialview01'>2qqf</scene>, resolution 2.0&Aring;
|SITE=
|SITE=
-
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=A1R:5&#39;-O-[(S)-{[(S)-{[(2R,3R,4S)-3,4-DIHYDROXYPYRROLIDIN-2-YL]METHOXY}(HYDROXY)PHOSPHORYL]OXY}(HYDROXY)PHOSPHORYL]ADENOSINE'>A1R</scene>
+
|LIGAND= <scene name='pdbligand=A1R:5&#39;-O-[(S)-{[(S)-{[(2R,3R,4S)-3,4-DIHYDROXYPYRROLIDIN-2-YL]METHOXY}(HYDROXY)PHOSPHORYL]OXY}(HYDROXY)PHOSPHORYL]ADENOSINE'>A1R</scene>, <scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= HST2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
|GENE= HST2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
 +
|DOMAIN=
 +
|RELATEDENTRY=[[2od7|2OD7]]
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qqf OCA], [http://www.ebi.ac.uk/pdbsum/2qqf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qqf RCSB]</span>
}}
}}
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[[Category: Slama, J.]]
[[Category: Slama, J.]]
[[Category: Zhao, K.]]
[[Category: Zhao, K.]]
-
[[Category: A1R]]
 
-
[[Category: ZN]]
 
[[Category: histone deacetylase]]
[[Category: histone deacetylase]]
[[Category: hst2]]
[[Category: hst2]]
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[[Category: zinc]]
[[Category: zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 15:46:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:52:05 2008''

Revision as of 01:52, 31 March 2008

Image:2qqf.jpg


PDB ID 2qqf

Drag the structure with the mouse to rotate
, resolution 2.0Å
Ligands: , ,
Gene: HST2 (Saccharomyces cerevisiae)
Related: 2OD7


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Hst2 bound to ADP-HPD and Acetylated histone H4


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

2QQF is a Protein complex structure of sequences 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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