› 2ptr

X-ray diffraction
1.85Å resolution

Crystal structure of Escherichia coli adenylosuccinate lyase mutant H171A with bound adenylosuccinate substrate

Released:
DOI: 10.2210/pdb2ptr/pdb
PDB entry 2ptr coloured by chain, front view.
PDB entry 2ptr coloured by chain, side view.
PDB entry 2ptr coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Substrate and product complexes of Escherichia coli adenylosuccinate lyase provide new insights into the enzymatic mechanism.
Tsai M, Koo J, Yip P, Colman RF, Segall ML, Howell PL
J Mol Biol 370 541-54 (2007)
PMID: 17531264

Function and Biology Details

Reaction catalysed: 
(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142028 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenylosuccinate lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 462 amino acids
Theoretical weight: 52.37 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AB89 (Residues: 1-456; Coverage: 100%)
Gene names: JW1117, b1131, purB
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 2SA 2 x 2SA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21212
Unit cell:
a: 98.4Å b: 143.19Å c: 69.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.183 0.216
Expression system: Escherichia coli

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Citations

3 review citations

Acyl-homoserine lactone-based quorum sensing in the Roseobacter clade: complex cell-to-cell communication controls multiple physiologies.
Cude et al. (2013)
2 more

6 mentions without citation

Structural biology of the purine biosynthetic pathway.
Zhang et al. (2008)
5 more