1ozb

X-ray diffraction
2.8Å resolution

Crystal Structure of SecB complexed with SecA C-terminus

Released:
Source organism: Haemophilus influenzae
Primary publication:
Structural determinants of SecB recognition by SecA in bacterial protein translocation.
Nat Struct Biol 10 942-7 (2003)
PMID: 14517549

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:

Structure analysis Details

Assemblies composition:
hetero hexamer (preferred)
homo tetramer
PDBe Complex ID:
PDB-CPX-155133 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein-export protein SecB Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 169 amino acids
Theoretical weight: 19.15 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P44853 (Residues: 1-169; Coverage: 100%)
Gene names: HI_0743, secB
Sequence domains: Preprotein translocase subunit SecB
Structure domains: SecB-like
Protein translocase subunit SecA Chains: I, J
Molecule details ›
Chains: I, J
Length: 27 amino acids
Theoretical weight: 3.03 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli
UniProt:
  • Canonical: P43803 (Residues: 875-901; Coverage: 3%)
Gene names: HI_0909, secA
Sequence domains: SEC-C motif

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P41212
Unit cell:
a: 114.5Å b: 114.5Å c: 286.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.226 0.273
Expression systems:
  • Escherichia coli BL21(DE3)
  • Escherichia coli