› 3q9l

X-ray diffraction
2.34Å resolution

The structure of the dimeric E.coli MinD-ATP complex

Released:
DOI: 10.2210/pdb3q9l/pdb
PDB entry 3q9l coloured by chain, front view.
PDB entry 3q9l coloured by chain, side view.
PDB entry 3q9l coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC.
Wu W, Park KT, Holyoak T, Lutkenhaus J
Mol Microbiol 79 1515-28 (2011)
PMID: 21231967

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142679 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Septum site-determining protein MinD Chains: A, B
Molecule details ›
Chains: A, B
Length: 260 amino acids
Theoretical weight: 28.5 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEZ3 (Residues: 1-260; Coverage: 96%)
Gene names: JW1164, b1175, minD
Sequence domains: CobQ/CobB/MinD/ParA nucleotide binding domain
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

2 bound ligands:
Ligand MG 2 x MG
Ligand ATP 2 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P212121
Unit cell:
a: 83.664Å b: 86.595Å c: 110.714Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.268 0.266 0.307
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Unusual biophysics of intrinsically disordered proteins.
Uversky VN. (2013)
10 more

19 mentions without citation

The ParA/MinD family puts things in their place.
Lutkenhaus J. (2012)
18 more