2B26

The crystal structure of the protein complex of yeast Hsp40 Sis1 and Hsp70 Ssa1


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.20 Å
  • R-Value Free: 0.339 
  • R-Value Work: 0.276 
  • R-Value Observed: 0.276 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Crystal structure of yeast Sis1 peptide-binding fragment and Hsp70 Ssa1 C-terminal complex.

Li, J.Wu, Y.Qian, X.Sha, B.

(2006) Biochem J 398: 353-360

  • DOI: https://doi.org/10.1042/BJ20060618
  • Primary Citation of Related Structures:  
    2B26

  • PubMed Abstract: 

    Heat shock protein (Hsp) 40 facilitates the critical role of Hsp70 in a number of cellular processes such as protein folding, assembly, degradation and translocation in vivo. Hsp40 and Hsp70 stay in close contact to achieve these diverse functions. The conserved C-terminal EEVD motif in Hsp70 has been shown to regulate Hsp40-Hsp70 interaction by an unknown mechanism. Here, we provide a structural basis for this regulation by determining the crystal structure of yeast Hsp40 Sis1 peptide-binding fragment complexed with the Hsp70 Ssa1 C-terminal. The Ssa1 extreme C-terminal eight residues, G634PTVEEVD641, form a beta-strand with the domain I of Sis1 peptide-binding fragment. Surprisingly, the Ssa1 C-terminal binds Sis1 at the site where Sis1 interacts with the non-native polypeptides. The negatively charged residues within the EEVD motif in Ssa1 C-terminal form extensive charge-charge interactions with the positively charged residues in Sis1. The structure-based mutagenesis data support the structural observations.


  • Organizational Affiliation

    Department of Cell Biology, Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, Brimingham, AL 35294-0005, USA.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
SIS1 protein
A, B, C
173Saccharomyces cerevisiaeMutation(s): 0 
Gene Names: SIS1
UniProt
Find proteins for P25294 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P25294 
Go to UniProtKB:  P25294
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP25294
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Heat shock 70 kDa protein cognate 27Drosophila melanogasterMutation(s): 0 
Gene Names: Hsc70-2Hsc2
UniProt
Find proteins for P11146 (Drosophila melanogaster)
Explore P11146 
Go to UniProtKB:  P11146
Entity Groups  
UniProt GroupP11146
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.20 Å
  • R-Value Free: 0.339 
  • R-Value Work: 0.276 
  • R-Value Observed: 0.276 
  • Space Group: P 41 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 113.867α = 90
b = 113.867β = 90
c = 173.881γ = 90
Software Package:
Software NamePurpose
HKL-2000data collection
SCALEPACKdata scaling
SOLVEphasing
CNSrefinement
HKL-2000data reduction

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-09-19
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2019-10-30
    Changes: Data collection, Database references, Derived calculations
  • Version 1.4: 2024-02-14
    Changes: Data collection, Database references