3Q35

Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated histone acetylation

Summary for 3Q35

Entry DOI	10.2210/pdb3q35/pdb
Related	3D35 3DM7 3Q33
Descriptor	Histone acetyltransferase, Vacuolar protein sorting-associated protein 75, ACETYL COENZYME *A, ... (5 entities in total)
Functional Keywords	rtt109:vps75=2:2 stoichiometry complex, acetyl coenzyme a (acoa) bound, autoacetylation at rtt109 lys290, nuclear, transferase-chaperone complex, transferase/chaperone
Biological source	Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast) More
Total number of polymer chains	2
Total formula weight	78513.22
Authors	Tang, Y.,Yuan, H.,Meeth, K.,Marmorstein, R. (deposition date: 2010-12-21, release date: 2011-02-02, Last modification date: 2023-12-06)
Primary citation	Tang, Y.,Holbert, M.A.,Delgoshaie, N.,Wurtele, H.,Guillemette, B.,Meeth, K.,Yuan, H.,Drogaris, P.,Lee, E.H.,Durette, C.,Thibault, P.,Verreault, A.,Cole, P.A.,Marmorstein, R. Structure of the Rtt109-AcCoA/Vps75 Complex and Implications for Chaperone-Mediated Histone Acetylation. Structure, 19:221-231, 2011 Cited by PubMed: 21256037 DOI: 10.1016/j.str.2010.12.012 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (3.3 Å)

Structure validation