› 3aeh

X-ray diffraction
2Å resolution

Integral membrane domain of autotransporter Hbp

Released:
DOI: 10.2210/pdb3aeh/pdb
PDB entry 3aeh coloured by chain, front view.
PDB entry 3aeh coloured by chain, side view.
PDB entry 3aeh coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
A novel intein-like autoproteolytic mechanism in autotransporter proteins.
Tajima N, Kawai F, Park SY, Tame JR
J Mol Biol 402 645-56 (2010)
PMID: 20615416

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131526 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hemoglobin-binding protease hbp translocator Chains: A, B
Molecule details ›
Chains: A, B
Length: 308 amino acids
Theoretical weight: 34.02 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: O88093 (Residues: 1075-1377; Coverage: 23%)
Gene name: hbp
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: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P21
Unit cell:
a: 73.011Å b: 68.893Å c: 78.378Å
α: 90° β: 117.75° γ: 90°
R-values:
R R work R free
0.177 0.175 0.222
Expression system: Escherichia coli

Quick links

Citations

11 review citations

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

12 mentions without citation

The structural biology of β-barrel membrane proteins: a summary of recent reports.
Fairman et al. (2011)
11 more