› 1nza

X-ray diffraction
1.7Å resolution

Divalent cation tolerance protein (Cut A1) from thermus thermophilus HB8

Released:
DOI: 10.2210/pdb1nza/pdb
PDB entry 1nza coloured by chain, front view.
PDB entry 1nza coloured by chain, side view.
PDB entry 1nza coloured by chain, top view.
Source organism: Thermus thermophilus
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 domain:

Structure analysis Details

Assemblies composition:
homo trimer (preferred)
homo dodecamer
Assembly name:
PDBe Complex ID:
PDB-CPX-181938 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Divalent-cation tolerance protein CutA Chain: A
Molecule details ›
Chain: A
Length: 103 amino acids
Theoretical weight: 11.64 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q7SIA8 (Residues: 1-103; Coverage: 100%)
Gene names: TTHA1356, 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 4 x CL
Ligand SO4 1 x SO4
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: I23
Unit cell:
a: 83.003Å b: 83.003Å c: 83.003Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.229 0.229 0.246
Expression system: Escherichia coli BL21(DE3)

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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

3 mentions without citation

Structure of a designed tetrahedral protein assembly variant engineered to have improved soluble expression.
Bale et al. (2015)
2 more