3Q66

Structure of the Vps75-Rtt109 histone chaperone-lysine acetyltransferase complex (Full-length proteins in space group P6122)

Summary for 3Q66

• Entry DOI: 10.2210/pdb3q66/pdb
• Related: 3Q68
• Descriptor: Vacuolar protein sorting-associated protein 75, Histone acetyltransferase RTT109, SULFATE ION, ... (4 entities in total)
• Functional Keywords: histone chaperone, lysine acetyltransferase, chaperone-transferase complex, chaperone/transferase
• Biological source: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast); More
• Cellular location: Nucleus: P53853 Q07794
• Total number of polymer chains: 3
• Total formula weight: 112310.76

Authors

Su, D.,Thompson, J.R.,Mer, G. (deposition date: 2010-12-30, release date: 2011-03-23, Last modification date: 2024-10-09)

Primary citation

Su, D.,Hu, Q.,Zhou, H.,Thompson, J.R.,Xu, R.M.,Zhang, Z.,Mer, G.
Structure and histone binding properties of the Vps75-Rtt109 chaperone-lysine acetyltransferase complex.
J.Biol.Chem., 286:15625-15629, 2011

PubMed Abstract: The histone chaperone Vps75 presents the remarkable property of stimulating the Rtt109-dependent acetylation of several histone H3 lysine residues within (H3-H4)(2) tetramers. To investigate this activation mechanism, we determined x-ray structures of full-length Vps75 in complex with full-length Rtt109 in two crystal forms. Both structures show similar asymmetric assemblies of a Vps75 dimer bound to an Rtt109 monomer. In the Vps75-Rtt109 complexes, the catalytic site of Rtt109 is confined to an enclosed space that can accommodate the N-terminal tail of histone H3 in (H3-H4)(2). Investigation of Vps75-Rtt109-(H3-H4)(2) and Vps75-(H3-H4)(2) complexes by NMR spectroscopy-probed hydrogen/deuterium exchange suggests that Vps75 guides histone H3 in the catalytic enclosure. These findings clarify the basis for the enhanced acetylation of histone H3 tail residues by Vps75-Rtt109.

PubMed: 21454705
DOI: 10.1074/jbc.C111.220715

Experimental method

X-RAY DIFFRACTION (2.705 Å)