6O22
| Structure of Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate. | Descriptor: | Histone H3.2, Histone H4, Histone acetyltransferase RTT109, ... | Authors: | Danilenko, N, Carlomagno, T, Kirkpatrick, J.P. | Deposit date: | 2019-02-22 | Release date: | 2019-07-31 | Last modified: | 2024-05-01 | Method: | SOLUTION NMR, SOLUTION SCATTERING | Cite: | Histone chaperone exploits intrinsic disorder to switch acetylation specificity. Nat Commun, 10, 2019
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6F0Y
| Rtt109 peptide bound to Asf1 | Descriptor: | Histone chaperone ASF1, histone acetyltransferase Rtt109 C-terminus | Authors: | Lercher, L, Kirkpatrick, J.P, Carlomagno, T. | Deposit date: | 2017-11-21 | Release date: | 2017-12-27 | Last modified: | 2024-05-15 | Method: | SOLUTION NMR | Cite: | Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation. Nucleic Acids Res., 46, 2018
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