› 3aqp

X-ray diffraction
3.3Å resolution

Crystal structure of SecDF, a translocon-associated membrane protein, from Thermus thrmophilus

Released:
DOI: 10.2210/pdb3aqp/pdb
PDB entry 3aqp coloured by chain, front view.
PDB entry 3aqp coloured by chain, side view.
PDB entry 3aqp coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Structure and function of a membrane component SecDF that enhances protein export.
Tsukazaki T, Mori H, Echizen Y, Ishitani R, Fukai S, Tanaka T, Perederina A, Vassylyev DG, Kohno T, Maturana AD, Ito K, Nureki O
Nature 474 235-8 (2011)
PMID: 21562494

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178083 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein translocase subunit SecDF Chains: A, B
Molecule details ›
Chains: A, B
Length: 741 amino acids
Theoretical weight: 80.59 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SKE6 (Residues: 1-735; Coverage: 100%)
Gene names: TTHA0697, secDF
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P43
Unit cell:
a: 140.636Å b: 140.636Å c: 160.563Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.299 0.298 0.319
Expression system: Escherichia coli

Quick links

Citations

39 review citations

Multidrug efflux pumps: structure, function and regulation.
Du et al. (2018)
38 more

16 mentions without citation

The bacterial Sec-translocase: structure and mechanism.
Lycklama A Nijeholt et al. (2012)
15 more