› 1m6n

X-ray diffraction
2.7Å resolution

Crystal structure of the SecA translocation ATPase from Bacillus subtilis

Released:
DOI: 10.2210/pdb1m6n/pdb
PDB entry 1m6n coloured by chain, front view.
PDB entry 1m6n coloured by chain, side view.
PDB entry 1m6n coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA.
Hunt JF, Weinkauf S, Henry L, Fak JJ, McNicholas P, Oliver DB, Deisenhofer J
Science 297 2018-26 (2002)
PMID: 12242434

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O + cellular protein(Side 1) = ADP + phosphate + cellular protein(Side 2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151218 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein translocase subunit SecA Chain: A
Molecule details ›
Chain: A
Length: 802 amino acids
Theoretical weight: 91.39 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P28366 (Residues: 1-802; Coverage: 95%)
Gene names: BSU35300, div+, secA
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 7 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID2
Spacegroup: P3112
Unit cell:
a: 130.833Å b: 130.833Å c: 150.35Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.22 0.22 0.301
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

44 review citations

Structure and mechanism of helicases and nucleic acid translocases.
Singleton et al. (2007)
43 more

38 mentions without citation

Interactions that drive Sec-dependent bacterial protein transport.
Rusch et al. (2007)
37 more