› 1hf2

X-ray diffraction
2.2Å resolution

Crystal structure of the bacterial cell-division inhibitor MinC from T. maritima

Released:
DOI: 10.2210/pdb1hf2/pdb
PDB entry 1hf2 coloured by chain, front view.
PDB entry 1hf2 coloured by chain, side view.
PDB entry 1hf2 coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Crystal structure of the bacterial cell division inhibitor MinC.
Cordell SC, Anderson RE, Löwe J
EMBO J 20 2454-61 (2001)
PMID: 11350934

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194700 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable septum site-determining protein MinC Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 210 amino acids
Theoretical weight: 22.76 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9X0D7 (Residues: 1-210; Coverage: 100%)
Gene names: TM_1047, minC
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 51.58Å b: 106.09Å c: 162.53Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.237 0.237 0.3
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

15 review citations

Cytokinesis in bacteria.
Errington et al. (2003)
14 more

11 mentions without citation

The E. coli MinCDE system in the regulation of protein patterns and gradients.
Ramm et al. (2019)
10 more