› 6t4h

X-ray diffraction
2.9Å resolution

Crystal structure of the accessory translocation ATPase, SecA2, from Clostridium difficile, in complex with adenosine-5'-(gamma-thio)-triphosphate

Released:
DOI: 10.2210/pdb6t4h/pdb
PDB entry 6t4h coloured by chain, front view.
PDB entry 6t4h coloured by chain, side view.
PDB entry 6t4h coloured by chain, top view.
Source organism: Clostridioides difficile 630
Primary publication:
The Structure of Clostridioides difficile SecA2 ATPase Exposes Regions Responsible for Differential Target Recognition of the SecA1 and SecA2-Dependent Systems.
Lindič N, Loboda J, Usenik A, Vidmar R, Turk D
OpenAccess logo Int J Mol Sci 21 (2020)
PMID: 32858965

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172681 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein translocase subunit SecA 2 Chain: A
Molecule details ›
Chain: A
Length: 781 amino acids
Theoretical weight: 89.25 KDa
Source organism: Clostridioides difficile 630
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q183M9 (Residues: 1-781; Coverage: 100%)
Gene names: CD630_27920, secA2
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand AGS 1 x AGS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 11.2C
Spacegroup: P212121
Unit cell:
a: 82.94Å b: 96.84Å c: 114.68Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.335 0.335 0.38
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 mention without citation

The Structure of Clostridioides difficile SecA2 ATPase Exposes Regions Responsible for Differential Target Recognition of the SecA1 and SecA2-Dependent Systems.
Lindič et al. (2020)