› 3qq2

X-ray diffraction
3Å resolution

Crystal Structure of the Beta Domain of the Bordetella Autotransporter Brka

Released:
DOI: 10.2210/pdb3qq2/pdb
PDB entry 3qq2 coloured by chain, front view.
PDB entry 3qq2 coloured by chain, side view.
PDB entry 3qq2 coloured by chain, top view.
Source organism: Bordetella pertussis
Primary publication:
Autotransporter passenger domain secretion requires a hydrophobic cavity at the extracellular entrance of the β-domain pore.
Zhai Y, Zhang K, Huo Y, Zhu Y, Zhou Q, Lu J, Black I, Pang X, Roszak AW, Zhang X, Isaacs NW, Sun F
Biochem J 435 577-87 (2011)
PMID: 21306302

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175049 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
BrkA translocator Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 284 amino acids
Theoretical weight: 30.99 KDa
Source organism: Bordetella pertussis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q45340 (Residues: 727-1010; Coverage: 29%)
Gene names: BP3494, brkA
Sequence domains: Autotransporter beta-domain
Structure domains: Autotransporter beta-domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: C2221
Unit cell:
a: 60.51Å b: 122.372Å c: 405.549Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.269 0.266 0.324
Expression system: Escherichia coli

Quick links

Citations

10 review citations

From self sufficiency to dependence: mechanisms and factors important for autotransporter biogenesis.
Leyton et al. (2012)
9 more

4 mentions without citation

Of linkers and autochaperones: an unambiguous nomenclature to identify common and uncommon themes for autotransporter secretion.
Drobnak et al. (2015)
3 more