› 1n1c

X-ray diffraction
2.4Å resolution

Crystal Structure Of The Dimeric TorD Chaperone From Shewanella Massilia

Released:
DOI: 10.2210/pdb1n1c/pdb
PDB entry 1n1c coloured by chain, front view.
PDB entry 1n1c coloured by chain, side view.
PDB entry 1n1c coloured by chain, top view.
Source organism: Shewanella massilia
Primary publication:
A novel protein fold and extreme domain swapping in the dimeric TorD chaperone from Shewanella massilia.
Tranier S, Iobbi-Nivol C, Birck C, Ilbert M, Mortier-Barrière I, Méjean V, Samama JP
Structure 11 165-74 (2003)
PMID: 12575936

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131522 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperone protein TorD Chains: A, B
Molecule details ›
Chains: A, B
Length: 217 amino acids
Theoretical weight: 24.65 KDa
Source organism: Shewanella massilia
Expression system: Escherichia coli
UniProt:
  • Canonical: O87949 (Residues: 1-209; Coverage: 100%)
Gene name: torD
Sequence domains: Nitrate reductase delta subunit
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand DTT 2 x DTT
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P212121
Unit cell:
a: 65.958Å b: 93.441Å c: 95.136Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.224 0.255
Expression system: Escherichia coli

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Citations

9 review citations

The bacterial twin-arginine translocation pathway.
Lee et al. (2006)
8 more

6 mentions without citation

The mononuclear molybdenum enzymes.
Hille et al. (2014)
5 more