2X26

Crystal structure of the periplasmic aliphatic sulphonate binding protein SsuA from Escherichia coli


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.75 Å
  • R-Value Free: 0.225 
  • R-Value Work: 0.186 
  • R-Value Observed: 0.188 

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This is version 1.3 of the entry. See complete history


Literature

Structure of the Aliphatic Sulfonate-Binding Protein Ssua from Escherichia Coli

Beale, J.Lee, S.Y.Iwata, S.Beis, K.

(2010) Acta Crystallogr Sect F Struct Biol Cryst Commun 66: 391

  • DOI: https://doi.org/10.1107/S1744309110006226
  • Primary Citation of Related Structures:  
    2X26

  • PubMed Abstract: 

    Sulfur is an essential component for the biosynthesis of the sulfur-containing amino acids L-methionine and L-cysteine. Under sulfur-starvation conditions, bacteria are capable of scavenging sulfur from sulfur-containing compounds and transporting it across membranes. Here, the crystal structure of the periplasmic aliphatic sulfonate-binding protein SsuA from Escherichia coli is reported at 1.75 A resolution in the substrate-free state. The overall structure of SsuA resembles the structures of other periplasmic binding proteins and contains two globular domains that form a cleft. Comparison with other periplasmic binding proteins revealed that one of the domains has been displaced by a rigid movement of 17 degrees . Interestingly, the tight crystal packing appears to be mediated by a 13-amino-acid tail from the cloning that folds within the cleft of the next monomer.


  • Organizational Affiliation

    Membrane Protein Laboratory, Diamond Light Source, Harwell Science and Innovation Campus, Oxfordshire OX11 0DE, England.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PERIPLASMIC ALIPHATIC SULPHONATES-BINDING PROTEIN
A, B
308Escherichia coli K-12Mutation(s): 0 
UniProt
Find proteins for P75853 (Escherichia coli (strain K12))
Explore P75853 
Go to UniProtKB:  P75853
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP75853
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.75 Å
  • R-Value Free: 0.225 
  • R-Value Work: 0.186 
  • R-Value Observed: 0.188 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 40.891α = 90
b = 96.026β = 90
c = 142.401γ = 90
Software Package:
Software NamePurpose
XDSdata reduction
SCALAdata scaling
BALBESphasing
MOLREPphasing
REFMACrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-04-14
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.2: 2019-03-06
    Changes: Data collection, Experimental preparation, Other
  • Version 1.3: 2023-12-20
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description