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3c9d
From Proteopedia
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
