3CYP

The crystal structure of the C-terminal domain of Helicobacter pylori MotB (residues 125-256).


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.227 
  • R-Value Work: 0.185 
  • R-Value Observed: 0.188 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Crystal structure of the cell wall anchor domain of MotB, a stator component of the bacterial flagellar motor: implications for peptidoglycan recognition.

Roujeinikova, A.

(2008) Proc Natl Acad Sci U S A 105: 10348-10353

  • DOI: https://doi.org/10.1073/pnas.0803039105
  • Primary Citation of Related Structures:  
    3CYP

  • PubMed Abstract: 

    The stator ring of the bacterial flagellar motor is composed of the MotA and MotB proteins that act together to generate a turning force (torque) acting on the FliG ring of the rotor. The C-terminal domain of MotB (MotB-C) is believed to anchor the MotA/MotB complex to peptidoglycan (PG) of the cell wall. The first crystal structures of MotB-C and its complex with N-acetylmuramic acid (NAM) have been determined to 1.6- and 2.3-A resolution, respectively. MotB-C is a dimer, both in solution and in the crystal. The two glycan chains of the PG ligand can be modeled as semirigid helices and docked into the grooves harboring the NAM molecules on the opposite faces of the dimer. The model suggests that a concave hydrophilic surface created upon edge-to-edge beta-sheet dimerization and centered around the 2-fold axis of the dimer can accommodate the peptide cross-bridge linking the two sugar chains. Significant structural similarities were found between MotB-C and the PG-binding domains of reduction-modifiable protein M and peptidoglycan-associated lipoprotein exclude, suggesting that PG recognition by different outer membrane protein A-like proteins may be governed by very similar molecular mechanisms that evidently involve protein dimerization.


  • Organizational Affiliation

    Manchester Interdisciplinary Biocenter, Faculty of Life Sciences, University of Manchester, 131 Princess Street, Manchester M1 7DN, United Kingdom.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Chemotaxis protein motBA [auth B],
B [auth C],
C [auth D],
D [auth E]
138Helicobacter pyloriMutation(s): 0 
Gene Names: motB
UniProt
Find proteins for P56427 (Helicobacter pylori (strain ATCC 700392 / 26695))
Explore P56427 
Go to UniProtKB:  P56427
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP56427
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.227 
  • R-Value Work: 0.185 
  • R-Value Observed: 0.188 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 50.816α = 90
b = 89.479β = 112.55
c = 66.322γ = 90
Software Package:
Software NamePurpose
SCALAdata scaling
REFMACrefinement
PDB_EXTRACTdata extraction
MOSFLMdata reduction
SHELXSphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2008-07-08
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2024-02-21
    Changes: Data collection, Database references