3UPV

TPR2B-domain:pHsp70-complex of yeast Sti1


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.254 
  • R-Value Work: 0.183 
  • R-Value Observed: 0.186 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop.

Schmid, A.B.Lagleder, S.Grawert, M.A.Rohl, A.Hagn, F.Wandinger, S.K.Cox, M.B.Demmer, O.Richter, K.Groll, M.Kessler, H.Buchner, J.

(2012) EMBO J 31: 1506-1517

  • DOI: https://doi.org/10.1038/emboj.2011.472
  • Primary Citation of Related Structures:  
    2LLV, 2LLW, 3UPV, 3UQ3

  • PubMed Abstract: 

    Sti1/Hop is a modular protein required for the transfer of client proteins from the Hsp70 to the Hsp90 chaperone system in eukaryotes. It binds Hsp70 and Hsp90 simultaneously via TPR (tetratricopeptide repeat) domains. Sti1/Hop contains three TPR domains (TPR1, TPR2A and TPR2B) and two domains of unknown structure (DP1 and DP2). We show that TPR2A is the high affinity Hsp90-binding site and TPR1 and TPR2B bind Hsp70 with moderate affinity. The DP domains exhibit highly homologous α-helical folds as determined by NMR. These, and especially DP2, are important for client activation in vivo. The core module of Sti1 for Hsp90 inhibition is the TPR2A-TPR2B segment. In the crystal structure, the two TPR domains are connected via a rigid linker orienting their peptide-binding sites in opposite directions and allowing the simultaneous binding of TPR2A to the Hsp90 C-terminal domain and of TPR2B to Hsp70. Both domains also interact with the Hsp90 middle domain. The accessory TPR1-DP1 module may serve as an Hsp70-client delivery system for the TPR2A-TPR2B-DP2 segment, which is required for client activation in vivo.


  • Organizational Affiliation

    Department Chemie, Center for Integrated Protein Science (CIPSM), Technische Universität München, Garching, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Heat shock protein STI1126Saccharomyces cerevisiae S288CMutation(s): 0 
Gene Names: STI1YOR027WOR26.17
UniProt
Find proteins for P15705 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P15705 
Go to UniProtKB:  P15705
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP15705
Sequence Annotations
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  • Reference Sequence

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Heat shock protein SSA47Saccharomyces cerevisiae S288CMutation(s): 0 
UniProt
Find proteins for P22202 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P22202 
Go to UniProtKB:  P22202
Entity Groups  
UniProt GroupP22202
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.254 
  • R-Value Work: 0.183 
  • R-Value Observed: 0.186 
  • Space Group: P 41 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 38.63α = 90
b = 38.63β = 90
c = 176.64γ = 90
Software Package:
Software NamePurpose
XDSdata scaling
PHASERphasing
REFMACrefinement
XDSdata reduction
XSCALEdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-01-25
    Type: Initial release
  • Version 1.1: 2012-04-04
    Changes: Database references
  • Version 1.2: 2023-09-13
    Changes: Data collection, Database references, Refinement description