6O22

Structure of Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate.

Summary for 6O22

• Entry DOI: 10.2210/pdb6o22/pdb
• NMR Information: BMRB: 30576
• Descriptor: Vacuolar protein sorting-associated protein 75, Histone acetyltransferase RTT109, Histone chaperone ASF1, ... (5 entities in total)
• Functional Keywords: chaperone
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 6
• Total formula weight: 170478.27

Authors

Danilenko, N.,Carlomagno, T.,Kirkpatrick, J.P. (deposition date: 2019-02-22, release date: 2019-07-31, Last modification date: 2024-05-01)

• Primary citation: Danilenko, N.,Lercher, L.,Kirkpatrick, J.,Gabel, F.,Codutti, L.,Carlomagno, T.; Histone chaperone exploits intrinsic disorder to switch acetylation specificity.; Nat Commun, 10:3435-3435, 2019; PubMed: 31387991; DOI: 10.1038/s41467-019-11410-7

Experimental method

SOLUTION NMR
SOLUTION SCATTERING