PDBsum entry 4cse

Chaperone

PDB id: 4cse

Contents

Protein chains

111 a.a.

Ligands

SER-GLU-LEU-ASP-SEP-ASP-ASP-GLU-PHE

ASP-SEP-ASP-ASP

Waters ×15

PDB id:

4cse

Name:

Chaperone

Title:

Pih n-terminal domain

Structure:

Pih1 domain-containing protein 1. Chain: a, b. Fragment: residues 47-179. Synonym: nucleolar protein 17 homolog, pih1d1. Engineered: yes. Telomere length regulation protein tel2 homolog. Chain: c, d. Fragment: residues 498-506. Engineered: yes

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 10090

Resolution:

3.30Å R-factor: 0.218 R-free: 0.306

Authors:

R.M.Morgan,S.M.Roe

Key ref:

M.Pal et al. (2014). Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1. Structure, 22, 805-818. PubMed id: 24794838 DOI: 10.1016/j.str.2014.04.001

Date:

07-Mar-14 Release date: 14-May-14

Protein chains

Q9CQJ2  (PIHD1_MOUSE) -  PIH1 domain-containing protein 1 from Mus musculus

Seq: 290 a.a.

Struc: 111 a.a.

DOI no: 10.1016/j.str.2014.04.001

Structure 22:805-818 (2014)

PubMed id: 24794838

Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1.

M.Pal, M.Morgan, S.E.Phelps, S.M.Roe, S.Parry-Morris, J.A.Downs, S.Polier, L.H.Pearl, C.Prodromou.

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.