› 3iqy

X-ray diffraction
3.3Å resolution

Active site mutants of B. subtilis SecA

Released:
DOI: 10.2210/pdb3iqy/pdb
PDB entry 3iqy coloured by chain, front view.
PDB entry 3iqy coloured by chain, side view.
PDB entry 3iqy coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
ATPase active-site electrostatic interactions control the global conformation of the 100 kDa SecA translocase.
Kim DM, Zheng H, Huang YJ, Montelione GT, Hunt JF
J Am Chem Soc 135 2999-3010 (2013)
PMID: 23167435

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 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: 841 amino acids
Theoretical weight: 95.63 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P28366 (Residues: 1-841; Coverage: 100%)
Gene names: BSU35300, div+, secA
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12B
Spacegroup: P3112
Unit cell:
a: 131.015Å b: 131.015Å c: 151.966Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.22 0.207 0.269
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Protein export through the bacterial Sec pathway.
Tsirigotaki et al. (2017)
3 more