› 1f1o

X-ray diffraction
3.25Å resolution

STRUCTURAL STUDIES OF ADENYLOSUCCINATE LYASES

Released:
DOI: 10.2210/pdb1f1o/pdb
PDB entry 1f1o coloured by chain, front view.
PDB entry 1f1o coloured by chain, side view.
PDB entry 1f1o coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds.
Toth EA, Worby C, Dixon JE, Goedken ER, Marqusee S, Yeates TO
J Mol Biol 301 433-50 (2000)
PMID: 10926519

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146084 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenylosuccinate lyase Chain: A
Molecule details ›
Chain: A
Length: 431 amino acids
Theoretical weight: 49.55 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P12047 (Residues: 1-431; Coverage: 100%)
Gene names: BSU06440, purB, purE
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P6522
Unit cell:
a: 129.53Å b: 129.53Å c: 282.08Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.336 0.336 0.355
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Posttranslational protein modification in Archaea.
Eichler et al. (2005)
10 more

2 mentions without citation

The Blueprint of a Minimal Cell: MiniBacillus.
Reuß et al. (2016)
1 more