4CGU: Full Length Tah1 Bound To Yeast Pih1 And Hsp90 Peptide Srmeevd

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.
PDB ID: 4CGUDownload
MMDB ID: 119329
PDB Deposition Date: 2013/11/26
Updated in MMDB: 2017/06
Experimental Method:
x-ray diffraction
Resolution: 2.11  Å
Source Organism:
Homo sapiens
Similar Structures:
Biological Unit for 4CGU: trimeric; determined by software (PISA)
Molecular Components in 4CGU
Label Count Molecule
Proteins (3 molecules)
TPR Repeat-containing Protein Associated With Hsp90(Gene symbol: TAH1)
Molecule annotation
Protein Interacting With Hsp90 1(Gene symbol: PIH1)
Molecule annotation
Heat Shock Protein HSP 90-alpha(Gene symbol: HSP90AA1)
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

Citing MMDB