› 4ys0

X-ray diffraction
1.9Å resolution

Conformational changes of the clamp of the protein translocation ATPase SecA from Thermotoga maritima

Released:
DOI: 10.2210/pdb4ys0/pdb
PDB 4ys0 coloured by chain and viewed from the front.
PDB 4ys0 coloured by chain and viewed from the side.
PDB 4ys0 coloured by chain and viewed from the top.
Source organism: Thermotoga maritima MSB8
Primary publication:
Conformational changes of the clamp of the protein translocation ATPase SecA.
Chen Y, Bauer BW, Rapoport TA, Gumbart JC
J. Mol. Biol. (2015)
PMID: 25982945

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein translocase subunit SecA Chain: A
Molecule details ›
Chain: A
Length: 824 amino acids
Theoretical weight: 95.17 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X1R4 (Residues: 1-816; Coverage: 94%)
Gene names: TM_1578, secA
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand ADP 1 x ADP
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P212121
Unit cell:
a: 64.404Å b: 110.16Å c: 115.863Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.179 0.226
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

5 mentions without citation

Co-Translational Protein Folding and Sorting in Chloroplasts.
Ries et al. (2020)
4 more