4CGU

Full length Tah1 bound to yeast PIH1 and HSP90 peptide SRMEEVD

Summary for 4CGU

• Entry DOI: 10.2210/pdb4cgu/pdb
• Related: 4CGV 4CGW 4CHH 4CKT 4CV4
• Descriptor: TPR REPEAT-CONTAINING PROTEIN ASSOCIATED WITH HSP90, PROTEIN INTERACTING WITH HSP90 1, HEAT SHOCK PROTEIN HSP 90-ALPHA, ... (5 entities in total)
• Functional Keywords: chaperone-peptide complex, chaperone, r2tp, tah1, hsp90, pih1, chaperone/peptide
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Cellular location: Cytoplasm : P25638 P38768 P07900
• Total number of polymer chains: 3
• Total formula weight: 31841.20

Authors

Roe, S.M.,Pal, M. (deposition date: 2013-11-26, release date: 2014-05-14, Last modification date: 2024-10-09)

Primary citation

Pal, M.,Morgan, M.,Phelps, S.E.,Roe, S.M.,Parry-Morris, S.,Downs, J.A.,Polier, S.,Pearl, L.H.,Prodromou, C.
Structural Basis for Phosphorylation-Dependent Recruitment of Tel2 to Hsp90 by Pih1.
Structure, 22:805-, 2014

PubMed Abstract: Client protein recruitment to the Hsp90 system depends on cochaperones that bind the client and Hsp90 simultaneously and facilitate their interaction. Hsp90 involvement in the assembly of snoRNPs, RNA polymerases, PI3-kinase-like kinases, and chromatin remodeling complexes depends on the TTT (Tel2-Tti1-Tti2), and R2TP complexes-consisting of the AAA-ATPases Rvb1 and Rvb2, Tah1 (Spagh/RPAP3 in metazoa), and Pih1 (Pih1D1 in humans)-that together provide the connection to Hsp90. The biochemistry underlying R2TP function is still poorly understood. Pih1 in particular, at the heart of the complex, has not been described at a structural level, nor have the multiple protein-protein interactions it mediates been characterized. Here we present a structural and biochemical analysis of Hsp90-Tah1-Pih1, Hsp90-Spagh, and Pih1D1-Tel2 complexes that reveal a domain in Pih1D1 specific for binding CK2 phosphorylation sites, and together define the structural basis by which the R2TP complex connects the Hsp90 chaperone system to the TTT complex.

PubMed: 24794838
DOI: 10.1016/J.STR.2014.04.001

Experimental method

X-RAY DIFFRACTION (2.11 Å)