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7L7I

Cryo-EM structure of Hsp90:FKBP51:p23 closed-state complex

Summary for 7L7I
Entry DOI10.2210/pdb7l7i/pdb
Related7L7J
EMDB information23213 23214
DescriptorPeptidyl-prolyl cis-trans isomerase FKBP5, Heat shock protein HSP 90-alpha, Prostaglandin E synthase 3, ... (4 entities in total)
Functional Keywordsisomerase-chaperone complex, isomerase/chaperone
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains4
Total formula weight240586.43
Authors
Lee, K.,Thwin, A.C.,Tse, E.,Gates, S.N.,Southworth, D.R. (deposition date: 2020-12-28, release date: 2021-08-25, Last modification date: 2024-05-29)
Primary citationLee, K.,Thwin, A.C.,Nadel, C.M.,Tse, E.,Gates, S.N.,Gestwicki, J.E.,Southworth, D.R.
The structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state.
Mol.Cell, 81:3496-, 2021
Cited by
PubMed Abstract: The Hsp90 chaperone promotes folding and activation of hundreds of client proteins in the cell through an ATP-dependent conformational cycle guided by distinct cochaperone regulators. The FKBP51 immunophilin binds Hsp90 with its tetratricopeptide repeat (TPR) domain and catalyzes peptidyl-prolyl isomerase (PPIase) activity during folding of kinases, nuclear receptors, and tau. Here we determined the cryoelectron microscopy (cryo-EM) structure of the human Hsp90:FKBP51:p23 complex to 3.3 Å, which, together with mutagenesis and crosslinking analyses, reveals the basis for cochaperone binding to Hsp90 during client maturation. A helix extension in the TPR functions as a key recognition element, interacting across the Hsp90 C-terminal dimer interface presented in the closed, ATP conformation. The PPIase domain is positioned along the middle domain, adjacent to Hsp90 client binding sites, whereas a single p23 makes stabilizing interactions with the N-terminal dimer. With this architecture, FKBP51 is positioned to act on specific client residues presented during Hsp90-catalyzed remodeling.
PubMed: 34380015
DOI: 10.1016/j.molcel.2021.07.023
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.3 Å)
Structure validation

239149

數據於2025-07-23公開中

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