3c9d
From Proteopedia
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{{STRUCTURE_3c9d| PDB=3c9d | SCENE= }} | {{STRUCTURE_3c9d| PDB=3c9d | SCENE= }} | ||
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===Crystal structure of Vps75=== | ===Crystal structure of Vps75=== | ||
+ | {{ABSTRACT_PUBMED_19172748}} | ||
- | + | ==Function== | |
+ | [[http://www.uniprot.org/uniprot/VPS75_YEAST VPS75_YEAST]] Histone chaperone which acts as a cofactor stimulating the histone H3 'Lys-56' acetylation by RTT109. May be involved in vacuolar proteins sorting.<ref>PMID:12134085</ref> <ref>PMID:17320445</ref> | ||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID:019172748</ref><references group="xtra"/> | + | <ref group="xtra">PMID:019172748</ref><references group="xtra"/><references/> |
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Berndsen, C E.]] | [[Category: Berndsen, C E.]] |
Revision as of 10:13, 3 July 2013
Contents |
Crystal structure of Vps75
Template:ABSTRACT PUBMED 19172748
Function
[VPS75_YEAST] Histone chaperone which acts as a cofactor stimulating the histone H3 'Lys-56' acetylation by RTT109. May be involved in vacuolar proteins sorting.[1] [2]
About this Structure
3c9d is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
- Berndsen CE, Tsubota T, Lindner SE, Lee S, Holton JM, Kaufman PD, Keck JL, Denu JM. Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75. Nat Struct Mol Biol. 2008 Sep;15(9):948-56. PMID:19172748
- ↑ Bonangelino CJ, Chavez EM, Bonifacino JS. Genomic screen for vacuolar protein sorting genes in Saccharomyces cerevisiae. Mol Biol Cell. 2002 Jul;13(7):2486-501. PMID:12134085 doi:http://dx.doi.org/10.1091/mbc.02-01-0005
- ↑ Tsubota T, Berndsen CE, Erkmann JA, Smith CL, Yang L, Freitas MA, Denu JM, Kaufman PD. Histone H3-K56 acetylation is catalyzed by histone chaperone-dependent complexes. Mol Cell. 2007 Mar 9;25(5):703-12. Epub 2007 Feb 22. PMID:17320445 doi:S1097-2765(07)00086-X