› 4nyo

X-ray diffraction
1.8Å resolution

The 1.8 Angstrom Crystal Structure of the Periplasmic Divalent Cation Tolerance Protein Cuta from Pyrococcus Horikoshii OT3

Released:
DOI: 10.2210/pdb4nyo/pdb
PDB entry 4nyo coloured by chain, front view.
PDB entry 4nyo coloured by chain, side view.
PDB entry 4nyo coloured by chain, top view.
Source organism: Pyrococcus horikoshii OT3
Primary publication:
The structures of the CutA1 proteins from Thermus thermophilus and Pyrococcus horikoshii: characterization of metal-binding sites and metal-induced assembly.
Bagautdinov B
Acta Crystallogr F Struct Biol Commun 70 404-13 (2014)
PMID: 24699729

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129759 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Divalent-cation tolerance protein CutA Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 102 amino acids
Theoretical weight: 12.4 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli
UniProt:
  • Canonical: O58720 (Residues: 1-102; Coverage: 100%)
Gene names: PH0992, cutA
Sequence domains: CutA1 divalent ion tolerance protein
Structure domains: Alpha-Beta Plaits

Ligands and Environments

4 bound ligands:
Ligand NA 2 x NA
Ligand CL 8 x CL
Ligand MES 4 x MES
Ligand SO4 2 x SO4
1 modified residue:
Ligand CSD 6 x CSD

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-D
Spacegroup: P212121
Unit cell:
a: 93.085Å b: 124.25Å c: 50.458Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 0.225
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Crystallographic studies on protein misfolding: Domain swapping and amyloid formation in the SH3 domain.
Cámara-Artigas A. (2016)
3 other articles

2 mentions without citation

The structures of the CutA1 proteins from Thermus thermophilus and Pyrococcus horikoshii: characterization of metal-binding sites and metal-induced assembly.
Bagautdinov B. (2014)
1 more