› 2v8d

X-ray diffraction
2.3Å resolution

Crystal structure of mutant E159A of beta-alanine synthase from Saccharomyces kluyveri

Released:
DOI: 10.2210/pdb2v8d/pdb
PDB entry 2v8d coloured by chain, front view.
PDB entry 2v8d coloured by chain, side view.
PDB entry 2v8d coloured by chain, top view.
Source organism: Lachancea kluyveri
Primary publication:
Crystal structures of yeast beta-alanine synthase complexes reveal the mode of substrate binding and large scale domain closure movements.
Lundgren S, Andersen B, Piskur J, Dobritzsch D
J Biol Chem 282 36037-47 (2007)
PMID: 17916556

Function and Biology Details

Reaction catalysed: 
3-ureidopropanoate + H(2)O = beta-alanine + CO(2) + NH(3)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188776 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase M20 dimerisation domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 474 amino acids
Theoretical weight: 51.95 KDa
Source organism: Lachancea kluyveri
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96W94 (Residues: 2-455; Coverage: 100%)
Gene name: PYD3
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 4 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 61.117Å b: 77.143Å c: 108.228Å
α: 90° β: 97.12° γ: 90°
R-values:
R R work R free
0.232 0.23 0.276
Expression system: Escherichia coli BL21(DE3)

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Citations

11 citation in other articles

The crystal structure of beta-alanine synthase from Drosophila melanogaster reveals a homooctameric helical turn-like assembly.
Lundgren et al. (2008)
10 more

2 mentions without citation

Structural and functional analyses reveal that Staphylococcus aureus antibiotic resistance factor HmrA is a zinc-dependent endopeptidase.
Botelho et al. (2011)
1 more