3Q33

Structure of the Rtt109-AcCoA/Vps75 Complex and Implications for Chaperone-Mediated Histone Acetylation

Summary for 3Q33

• Entry DOI: 10.2210/pdb3q33/pdb
• Related: 3D35 3DM7 3Q35
• Descriptor: Histone acetyltransferase RTT109, Vacuolar protein sorting-associated protein 75, HISTONE H3, ... (6 entities in total)
• Functional Keywords: rtt109:vps75=2:2 stoichiometry complex, histone acetyltransferase, with acetyl coenzyme a (acoa) bound, autoacetylation on rtt109 lys290, nuclear, transferase-chaperone-transcription regulator complex, transferase-chaperone complex, transferase, chaperone-gene regulation complex, chaperone/gene regulation
• Biological source: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast); More
• Cellular location: Nucleus: Q07794 P53853 P61830
• Total number of polymer chains: 3
• Total formula weight: 80005.95

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; PubMed: 21256037; DOI: 10.1016/j.str.2010.12.012

Experimental method

X-RAY DIFFRACTION (2.8 Å)