› 2xtr

X-ray diffraction
2.14Å resolution

Structure of the P176A Colicin M mutant from E. coli

Released:
DOI: 10.2210/pdb2xtr/pdb
PDB entry 2xtr coloured by chain, front view.
PDB entry 2xtr coloured by chain, side view.
PDB entry 2xtr 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
Molecule details ›
Chains: A, B
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

1 bound ligand:
Ligand NO3 1 x NO3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: C2221
Unit cell:
a: 52.832Å b: 114.772Å c: 225.402Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.188 0.241
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

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

2 mentions 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)
1 more