1ELR

Crystal structure of the TPR2A domain of HOP in complex with the HSP90 peptide MEEVD


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.219 
  • R-Value Work: 0.181 
  • R-Value Observed: 0.181 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine.

Scheufler, C.Brinker, A.Bourenkov, G.Pegoraro, S.Moroder, L.Bartunik, H.Hartl, F.U.Moarefi, I.

(2000) Cell 101: 199-210

  • DOI: https://doi.org/10.1016/S0092-8674(00)80830-2
  • Primary Citation of Related Structures:  
    1ELR, 1ELW

  • PubMed Abstract: 

    The adaptor protein Hop mediates the association of the molecular chaperones Hsp70 and Hsp90. The TPR1 domain of Hop specifically recognizes the C-terminal heptapeptide of Hsp70 while the TPR2A domain binds the C-terminal pentapeptide of Hsp90. Both sequences end with the motif EEVD. The crystal structures of the TPR-peptide complexes show the peptides in an extended conformation, spanning a groove in the TPR domains. Peptide binding is mediated by electrostatic interactions with the EEVD motif, with the C-terminal aspartate acting as a two-carboxylate anchor, and by hydrophobic interactions with residues upstream of EEVD. The hydrophobic contacts with the peptide are critical for specificity. These results explain how TPR domains participate in the ordered assembly of Hsp70-Hsp90 multichaperone complexes.


  • Organizational Affiliation

    Max-Planck Institute for Biochemistry, Martinsried, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
TPR2A-DOMAIN OF HOP131Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P31948 (Homo sapiens)
Explore P31948 
Go to UniProtKB:  P31948
PHAROS:  P31948
GTEx:  ENSG00000168439 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP31948
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
HSP90-PEPTIDE MEEVD6N/AMutation(s): 0 
UniProt
Find proteins for Q9H2A1 (Homo sapiens)
Explore Q9H2A1 
Go to UniProtKB:  Q9H2A1
Entity Groups  
UniProt GroupQ9H2A1
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
NI
Query on NI

Download Ideal Coordinates CCD File 
C [auth A]NICKEL (II) ION
Ni
VEQPNABPJHWNSG-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.219 
  • R-Value Work: 0.181 
  • R-Value Observed: 0.181 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 73.28α = 90
b = 48.27β = 91.3
c = 38.06γ = 90
Software Package:
Software NamePurpose
MAR345data collection
XDSdata reduction
MLPHAREphasing
CNSrefinement
XDSdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-04-26
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2017-10-04
    Changes: Refinement description