› 1ev0

Solution NMR

SOLUTION STRUCTURE OF THE MINE TOPOLOGICAL SPECIFICITY DOMAIN

Released:
DOI: 10.2210/pdb1ev0/pdb
PDB entry 1ev0 coloured by chain, ensemble of 20 models, front view.
PDB entry 1ev0 coloured by chain, ensemble of 20 models, side view.
PDB entry 1ev0 coloured by chain, ensemble of 20 models, top view.
Source organism: Escherichia coli
Primary publication:
Structural basis for the topological specificity function of MinE.
King GF, Shih YL, Maciejewski MW, Bains NP, Pan B, Rowland SL, Mullen GP, Rothfield LI
Nat Struct Biol 7 1013-7 (2000)
PMID: 11062554

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141520 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cell division topological specificity factor Chains: A, B
Molecule details ›
Chains: A, B
Length: 58 amino acids
Theoretical weight: 6.71 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A734 (Residues: 31-88; Coverage: 66%)
Gene names: JW1163, b1174, minE
Sequence domains: Septum formation topological specificity factor MinE
Structure domains: Cell division topological specificity factor MinE

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics followed by dynamical simulated annealing
Expression system: Escherichia coli

Quick links

Citations

13 review citations

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

11 mentions without citation

The Min oscillator uses MinD-dependent conformational changes in MinE to spatially regulate cytokinesis.
Park et al. (2011)
10 more