4CSE

PIH N-terminal domain

Summary for 4CSE

• Entry DOI: 10.2210/pdb4cse/pdb
• Related: 4CGU 4CGV 4CGW 4CHH 4CKT 4CV4
• Descriptor: PIH1 DOMAIN-CONTAINING PROTEIN 1, TELOMERE LENGTH REGULATION PROTEIN TEL2 HOMOLOG (3 entities in total)
• Functional Keywords: chaperone, molecular chaperones, multiprotein complexes, phosphorylation
• Biological source: MUS MUSCULUS (HOUSE MOUSE); More
• Cellular location: Cytoplasm (By similarity): Q9DC40
• Total number of polymer chains: 4
• Total formula weight: 32225.79

Authors

Morgan, R.M.,Roe, S.M. (deposition date: 2014-03-07, release date: 2014-05-14, Last modification date: 2024-10-23)

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 (3.3 Å)