› 2be7

X-ray diffraction
2.85Å resolution

Crystal structure of the unliganded (T-state) aspartate transcarbamoylase of the psychrophilic bacterium Moritella profunda

Released:
DOI: 10.2210/pdb2be7/pdb
PDB entry 2be7 coloured by chain, front view.
PDB entry 2be7 coloured by chain, side view.
PDB entry 2be7 coloured by chain, top view.
Source organism: Moritella profunda
Primary publication:
Structural investigation of cold activity and regulation of aspartate carbamoyltransferase from the extreme psychrophilic bacterium Moritella profunda.
De Vos D, Xu Y, Hulpiau P, Vergauwen B, Van Beeumen JJ
J Mol Biol 365 379-95 (2007)
PMID: 17070547

Function and Biology Details

Reaction catalysed: 
Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112126 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Aspartate carbamoyltransferase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 326 amino acids
Theoretical weight: 36.27 KDa
Source organism: Moritella profunda
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: D0VWV8 (Residues: 1-310; Coverage: 100%)
Gene name: pyrB
Sequence domains:
Structure domains: Aspartate/ornithine carbamoyltransferase
Aspartate carbamoyltransferase regulatory chain Chains: D, E, F
Molecule details ›
Chains: D, E, F
Length: 153 amino acids
Theoretical weight: 16.91 KDa
Source organism: Moritella profunda
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: D0VWV9 (Residues: 1-153; Coverage: 100%)
Gene name: pyrI
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 3 x SO4
Ligand ZN 3 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P3221
Unit cell:
a: 129.238Å b: 129.238Å c: 207.232Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.214 0.212 0.257
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Thermodynamic and functional characteristics of deep-sea enzymes revealed by pressure effects.
Ohmae et al. (2013)
2 more

5 mentions without citation

Psychrophilic enzymes: from folding to function and biotechnology.
Feller G. (2013)
4 more