› 1tf5

X-ray diffraction
2.18Å resolution

Crystal structure of SecA in an open conformation from Bacillus Subtilis

Released:
DOI: 10.2210/pdb1tf5/pdb
PDB entry 1tf5 coloured by chain, front view.
PDB entry 1tf5 coloured by chain, side view.
PDB entry 1tf5 coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
A large conformational change of the translocation ATPase SecA.
Osborne AR, Clemons WM, Rapoport TA
Proc Natl Acad Sci U S A 101 10937-42 (2004)
PMID: 15256599

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151216 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein translocase subunit SecA Chain: A
Molecule details ›
Chain: A
Length: 844 amino acids
Theoretical weight: 95.96 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P28366 (Residues: 1-841; Coverage: 100%)
Gene names: BSU35300, div+, secA
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2
Unit cell:
a: 149.232Å b: 107.189Å c: 72.054Å
α: 90° β: 94.96° γ: 90°
R-values:
R R work R free
0.241 0.241 0.273
Expression system: Escherichia coli

Quick links

Citations

26 review citations

The DEAD-box protein family of RNA helicases.
Cordin et al. (2006)
25 more

22 mentions without citation

Targeting Metalloenzymes for Therapeutic Intervention.
Chen et al. (2019)
21 more