2ZD7
The structure of VPS75 (Vacuolar protein sorting-associated protein 75)
Summary for 2ZD7
| Entry DOI | 10.2210/pdb2zd7/pdb |
| Descriptor | Vacuolar protein sorting-associated protein 75, EVDLPLSDEEPSS (3 entities in total) |
| Functional Keywords | histone chaperone, vps75, nap1, nucleus, phosphoprotein, protein transport, transport |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
| Total number of polymer chains | 3 |
| Total formula weight | 62728.61 |
| Authors | Park, Y.J.,Luger, K. (deposition date: 2007-11-20, release date: 2008-08-12, Last modification date: 2024-03-13) |
| Primary citation | Park, Y.J.,Sudhoff, K.B.,Andrews, A.J.,Stargell, L.A.,Luger, K. Histone chaperone specificity in Rtt109 activation. Nat.Struct.Mol.Biol., 15:957-964, 2008 Cited by PubMed Abstract: Rtt109 is a histone acetyltransferase that requires a histone chaperone for the acetylation of histone 3 at lysine 56 (H3K56). Rtt109 forms a complex with the chaperone Vps75 in vivo and is implicated in DNA replication and repair. Here we show that both Rtt109 and Vps75 bind histones with high affinity, but only the complex is efficient for catalysis. The C-terminal acidic domain of Vps75 contributes to activation of Rtt109 and is necessary for in vivo functionality of Vps75, but it is not required for interaction with either Rtt109 or histones. We demonstrate that Vps75 is a structural homolog of yeast Nap1 by solving its crystal structure. Nap1 and Vps75 interact with histones and Rtt109 with comparable affinities. However, only Vps75 stimulates Rtt109 enzymatic activity. Our data highlight the functional specificity of Vps75 in Rtt109 activation. PubMed: 19172749DOI: 10.1038/nsmb.1480 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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