› 2l16

Solution NMR

Solution structure of Bacillus subtilits TatAd protein in DPC micelles

Released:
DOI: 10.2210/pdb2l16/pdb
PDB entry 2l16 coloured by chain, ensemble of 40 models, front view.
PDB entry 2l16 coloured by chain, ensemble of 40 models, side view.
PDB entry 2l16 coloured by chain, ensemble of 40 models, top view.
Source organism: Bacillus subtilis
Primary publication:
Solution NMR structure of the TatA component of the twin-arginine protein transport system from gram-positive bacterium Bacillus subtilis.
Hu Y, Zhao E, Li H, Xia B, Jin C
J Am Chem Soc 132 15942-4 (2010)
PMID: 20726548

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-128294 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sec-independent protein translocase protein TatAd Chain: A
Molecule details ›
Chain: A
Length: 78 amino acids
Theoretical weight: 8.51 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: O31467 (Residues: 1-70; Coverage: 100%)
Gene names: BSU02630, tatAd, yczB
Sequence domains: mttA/Hcf106 family
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

15 review citations

The twin-arginine translocation (Tat) protein export pathway.
Palmer et al. (2012)
14 more

2 mentions without citation

Molecular dissection of TatC defines critical regions essential for protein transport and a TatB-TatC contact site.
Kneuper et al. (2012)
1 more