› 5a0g

X-ray diffraction
2.62Å resolution

N-terminal thioester domain of surface protein from Clostridium perfringens

Released:
DOI: 10.2210/pdb5a0g/pdb
PDB entry 5a0g coloured by chain, front view.
PDB entry 5a0g coloured by chain, side view.
PDB entry 5a0g coloured by chain, top view.
Source organism: Clostridium perfringens B
Primary publication:
An internal thioester in a pathogen surface protein mediates covalent host binding.
Walden M, Edwards JM, Dziewulska AM, Bergmann R, Saalbach G, Kan SY, Miller OK, Weckener M, Jackson RJ, Shirran SL, Botting CH, Florence GJ, Rohde M, Banfield MJ, Schwarz-Linek U
Elife 4 (2015)
PMID: 26032562

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109411 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative surface anchored protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 188 amino acids
Theoretical weight: 21.28 KDa
Source organism: Clostridium perfringens B
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B1R775 (Residues: 92-277; Coverage: 9%)
Gene name: AC1_0147
Sequence domains: Thioester domain
Structure domains: Thioester domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P1
Unit cell:
a: 70.82Å b: 74.36Å c: 82.81Å
α: 107.32° β: 104.32° γ: 98.63°
R-values:
R R work R free
0.198 0.196 0.226
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Engineering of Metabolic Pathways by Artificial Enzyme Channels.
Pröschel et al. (2015)
5 more

2 mentions without citation

An internal thioester in a pathogen surface protein mediates covalent host binding.
Walden et al. (2015)
1 more