› 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 1tf5 coloured by chain and viewed from the front.
PDB 1tf5 coloured by chain and viewed from the side.
PDB 1tf5 coloured by chain and viewed from the top.
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)
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

24 review citations

Single-Molecule Studies on the Protein Translocon.
Seinen et al. (2019)
23 more

21 mentions without citation

The Sec System: Protein Export in Escherichia coli.
Crane et al. (2017)
20 more