1YFN

Versatile modes of peptide recognition by the AAA+ adaptor protein SspB- the crystal structure of a SspB-RseA complex


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.261 
  • R-Value Work: 0.234 
  • R-Value Observed: 0.241 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Versatile modes of peptide recognition by the AAA+ adaptor protein SspB

Levchenko, I.Grant, R.A.Flynn, J.M.Sauer, R.T.Baker, T.A.

(2005) Nat Struct Mol Biol 12: 520-525

  • DOI: https://doi.org/10.1038/nsmb934
  • Primary Citation of Related Structures:  
    1YFN

  • PubMed Abstract: 

    Energy-dependent proteases often rely on adaptor proteins to modulate substrate recognition. The SspB adaptor binds peptide sequences in the stress-response regulator RseA and in ssrA-tagged proteins and delivers these molecules to the AAA+ ClpXP protease for degradation. The structure of SspB bound to an ssrA peptide is known. Here, we report the crystal structure of a complex between SspB and its recognition peptide in RseA. Notably, the RseA sequence is positioned in the peptide-binding groove of SspB in a direction opposite to the ssrA peptide, the two peptides share only one common interaction with the adaptor, and the RseA interaction site is substantially larger than the overlapping ssrA site. This marked diversity in SspB recognition of different target proteins indicates that it is capable of highly flexible and dynamic substrate delivery.


  • Organizational Affiliation

    Department of Biology, Massachusetts Institute of Technology, 68-523, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Stringent starvation protein B
A, B, C, D
118Escherichia coliMutation(s): 0 
UniProt
Find proteins for P0AFZ3 (Escherichia coli (strain K12))
Explore P0AFZ3 
Go to UniProtKB:  P0AFZ3
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0AFZ3
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Sigma-E factor negative regulatory protein
E, F, G, H
32N/AMutation(s): 0 
UniProt
Find proteins for P0AFX7 (Escherichia coli (strain K12))
Explore P0AFX7 
Go to UniProtKB:  P0AFX7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0AFX7
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.261 
  • R-Value Work: 0.234 
  • R-Value Observed: 0.241 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 69.647α = 90
b = 60.533β = 94.62
c = 88.576γ = 90
Software Package:
Software NamePurpose
CNSrefinement
HKL-2000data reduction
SCALEPACKdata scaling
AMoREphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-05-17
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-08-23
    Changes: Data collection, Database references, Refinement description