1q14
From Proteopedia
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|PDB= 1q14 |SIZE=350|CAPTION= <scene name='initialview01'>1q14</scene>, resolution 2.5Å | |PDB= 1q14 |SIZE=350|CAPTION= <scene name='initialview01'>1q14</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= PROD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= PROD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q14 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q14 OCA], [http://www.ebi.ac.uk/pdbsum/1q14 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q14 RCSB]</span> | ||
}} | }} | ||
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[[Category: Marmorstein, R.]] | [[Category: Marmorstein, R.]] | ||
[[Category: Zhao, K.]] | [[Category: Zhao, K.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: ZN]] | ||
[[Category: histone deacetylase]] | [[Category: histone deacetylase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:07:23 2008'' |
Revision as of 20:07, 30 March 2008
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| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | PROD (Saccharomyces cerevisiae) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure and autoregulation of the yeast Hst2 homolog of Sir2
Overview
Yeast Hst2 (yHst2) is a member of the silencing information regulator 2 (Sir2) family of NAD(+)-dependent protein deacetylases that are implicated in transcriptional silencing, DNA repair, genome stability and longevity. The X-ray crystal structure of the full-length yHst2 protein reveals a central catalytic core domain fold that is characteristic of the other Sir2 homologs, and C- and N-terminal extensions that interact with the NAD(+) and acetyl-lysine substrate-binding sites, respectively, suggesting an autoregulatory function for these domains. Moreover, the N-terminal extension mediates formation of a homotrimer within the crystal lattice. Enzymatic and sedimentation equilibrium studies using deletion constructs of yHst2 support the involvement of the N- and C-terminal yHst2 regions and trimer formation in catalysis by yHst2. Together, these studies indicate that the sequence-divergent N- and C-terminal regions of the eukaryotic Sir2 proteins may have a particularly important role in their distinct substrate-binding properties, biological activities or both.
About this Structure
1Q14 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structure and autoregulation of the yeast Hst2 homolog of Sir2., Zhao K, Chai X, Clements A, Marmorstein R, Nat Struct Biol. 2003 Oct;10(10):864-71. Epub 2003 Sep 21. PMID:14502267
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