› 3da3

X-ray diffraction
2.5Å resolution

Crystal Structure of Colicin M, A Novel Phosphatase Specifically Imported by Escherichia Coli

Released:
DOI: 10.2210/pdb3da3/pdb
PDB entry 3da3 coloured by chain, front view.
PDB entry 3da3 coloured by chain, side view.
PDB entry 3da3 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of colicin M, a novel phosphatase specifically imported by Escherichia coli.
Zeth K, Römer C, Patzer SI, Braun V
J Biol Chem 283 25324-25331 (2008)
PMID: 18640984

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
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: 278 amino acids
Theoretical weight: 30.41 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P05820 (Residues: 1-271; Coverage: 100%)
Gene name: cma
Sequence domains: Colicin M
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P42212
Unit cell:
a: 119.88Å b: 119.88Å c: 96.22Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.235 0.295
Expression system: Escherichia coli

Quick links

Citations

15 review citations

TonB-dependent transporters: regulation, structure, and function.
Noinaj et al. (2010)
14 more

3 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)
2 more