3s0h

X-ray diffraction
2.1Å resolution

The crystal structure of the periplasmic domain of Helicobacter pylori MotB (residues 90-256).

Released:
Source organism: Helicobacter pylori
Primary publication:
Role of the MotB linker in the assembly and activation of the bacterial flagellar motor.
Acta Crystallogr D Biol Crystallogr 67 1009-16 (2011)
PMID: 22120737

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-157470 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Motility protein B Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 173 amino acids
Theoretical weight: 19.67 KDa
Source organism: Helicobacter pylori
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P56427 (Residues: 91-257; Coverage: 65%)
Gene names: HP_0816, motB
Sequence domains: OmpA family
Structure domains: OmpA-like domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P43
Unit cell:
a: 72.972Å b: 72.972Å c: 127.178Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.181 0.236
Expression system: Escherichia coli BL21