› 2wqk

X-ray diffraction
1.5Å resolution

Crystal Structure of Sure Protein from Aquifex aeolicus

Released:
DOI: 10.2210/pdb2wqk/pdb
PDB entry 2wqk coloured by chain, front view.
PDB entry 2wqk coloured by chain, side view.
PDB entry 2wqk coloured by chain, top view.
Source organism: Aquifex aeolicus VF5
Primary publication:
Structure of SurE protein from Aquifex aeolicus VF5 at 1.5 A resolution.
Antonyuk SV, Ellis MJ, Strange RW, Bessho Y, Kuramitsu S, Shinkai A, Yokoyama S, Hasnain SS
Acta Crystallogr Sect F Struct Biol Cryst Commun 65 1204-8 (2009)
PMID: 20054112

Function and Biology Details

Reaction catalysed: 
A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130407 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
5'-nucleotidase SurE Chains: A, B
Molecule details ›
Chains: A, B
Length: 251 amino acids
Theoretical weight: 28.2 KDa
Source organism: Aquifex aeolicus VF5
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O67004 (Residues: 1-251; Coverage: 100%)
Gene names: aq_832, surE
Sequence domains: Survival protein SurE
Structure domains: Survival protein SurE-like phosphatase/nucleotidase

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX10.1
Spacegroup: P3221
Unit cell:
a: 65.006Å b: 65.006Å c: 239.194Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.157 0.156 0.191
Expression system: Escherichia coli BL21(DE3)

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Citations

1 citations in other articles

Conformational variability of the stationary phase survival protein E from Xylella fastidiosa revealed by X-ray crystallography, small-angle X-ray scattering studies, and normal mode analysis.
Machado et al. (2017)

5 mentions without citation

Dramatic structural changes resulting from the loss of a crucial hydrogen bond in the hinge region involved in C-terminal helix swapping in SurE: a survival protein from Salmonella typhimurium.
Mathiharan et al. (2013)
4 more