› 3iqc

X-ray diffraction
2.7Å resolution

Crystal structure of FliS from H. pylori

Released:
DOI: 10.2210/pdb3iqc/pdb
PDB entry 3iqc coloured by chain, front view.
PDB entry 3iqc coloured by chain, side view.
PDB entry 3iqc coloured by chain, top view.
Source organism: Helicobacter pylori 26695
Primary publication:
Molecular interaction of flagellar export chaperone FliS and cochaperone HP1076 in Helicobacter pylori.
Lam WW, Woo EJ, Kotaka M, Tam WK, Leung YC, Ling TK, Au SW
FASEB J 24 4020-32 (2010)
PMID: 20581225

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-127751 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Flagellar secretion chaperone FliS Chains: A, B
Molecule details ›
Chains: A, B
Length: 131 amino acids
Theoretical weight: 14.97 KDa
Source organism: Helicobacter pylori 26695
Expression system: Escherichia coli
UniProt:
  • Canonical: O25448 (Residues: 1-126; Coverage: 100%)
Gene name: HP_0753
Sequence domains: Flagellar protein FliS
Structure domains: Flagellar protein FliS

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: I4122
Unit cell:
a: 92.469Å b: 92.469Å c: 144.292Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.238 0.284
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Role of Flagella in the Pathogenesis of Helicobacter pylori.
Gu H. (2017)
1 more

2 mentions without citation

Structural Conservation and Adaptation of the Bacterial Flagella Motor.
Carroll et al. (2020)
1 more