› 2xtq

X-ray diffraction
2.31Å resolution

Structure of the P107A Colicin M mutant from E. coli

Released:
DOI: 10.2210/pdb2xtq/pdb
PDB entry 2xtq coloured by chain, front view.
PDB entry 2xtq coloured by chain, side view.
PDB entry 2xtq coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Activation of colicin M by the FkpA prolyl cis-trans isomerase/chaperone.
Helbig S, Patzer SI, Schiene-Fischer C, Zeth K, Braun V
J Biol Chem 286 6280-90 (2011)
PMID: 21149455

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138790 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Colicin-M Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 271 amino acids
Theoretical weight: 29.49 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P05820 (Residues: 1-271; Coverage: 100%)
Gene name: cma
Sequence domains: Colicin M
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P1
Unit cell:
a: 52.852Å b: 63.114Å c: 189.34Å
α: 87.59° β: 82.17° γ: 65.65°
R-values:
R R work R free
0.242 0.24 0.273
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

The Bam machine: a molecular cooper.
Ricci et al. (2012)
8 more

1 mention without citation

The crystal structure of the lipid II-degrading bacteriocin syringacin M suggests unexpected evolutionary relationships between colicin M-like bacteriocins.
Grinter et al. (2012)