6F0Y
Rtt109 peptide bound to Asf1
Summary for 6F0Y
| Entry DOI | 10.2210/pdb6f0y/pdb |
| NMR Information | BMRB: 34201 |
| Descriptor | Histone chaperone ASF1, histone acetyltransferase Rtt109 C-terminus (2 entities in total) |
| Functional Keywords | histone chaperone, acetyl transferase, transferase |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
| Total number of polymer chains | 2 |
| Total formula weight | 21014.86 |
| Authors | Lercher, L.,Kirkpatrick, J.P.,Carlomagno, T. (deposition date: 2017-11-21, release date: 2017-12-27, Last modification date: 2024-05-15) |
| Primary citation | Lercher, L.,Danilenko, N.,Kirkpatrick, J.,Carlomagno, T. Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation. Nucleic Acids Res., 46:2279-2289, 2018 Cited by PubMed Abstract: Acetylation of histone H3 at lysine-56 by the histone acetyltransferase Rtt109 in lower eukaryotes is important for maintaining genomic integrity and is required for C. albicans pathogenicity. Rtt109 is activated by association with two different histone chaperones, Vps75 and Asf1, through an unknown mechanism. Here, we reveal that the Rtt109 C-terminus interacts directly with Asf1 and elucidate the structural basis of this interaction. In addition, we find that the H3 N-terminus can interact via the same interface on Asf1, leading to a competition between the two interaction partners. This, together with the recruitment and position of the substrate, provides an explanation of the role of the Rtt109 C-terminus in Asf1-dependent Rtt109 activation. PubMed: 29300933DOI: 10.1093/nar/gkx1283 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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