› 1s0a

X-ray diffraction
1.71Å resolution

Crystal Structure of the Y17F Mutant of 7,8-Diaminopelargonic Acid Synthase

Released:
DOI: 10.2210/pdb1s0a/pdb
PDB entry 1s0a coloured by chain, front view.
PDB entry 1s0a coloured by chain, side view.
PDB entry 1s0a coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Conserved and nonconserved residues in the substrate binding site of 7,8-diaminopelargonic acid synthase from Escherichia coli are essential for catalysis.
Sandmark J, Eliot AC, Famm K, Schneider G, Kirsch JF
Biochemistry 43 1213-22 (2004)
PMID: 14756557

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146421 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenosylmethionine-8-amino-7-oxononanoate aminotransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 429 amino acids
Theoretical weight: 47.52 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P12995 (Residues: 1-429; Coverage: 100%)
Gene names: JW0757, b0774, bioA
Sequence domains: Aminotransferase class-III
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand NA 2 x NA
1 modified residue:
Ligand LLP 2 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P21
Unit cell:
a: 58.508Å b: 55.659Å c: 121.396Å
α: 90° β: 97.04° γ: 90°
R-values:
R R work R free
0.19 0.186 0.206
Expression system: Escherichia coli BL21(DE3)

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Citations

4 review citations

Bioinformatic analysis of a PLP-dependent enzyme superfamily suitable for biocatalytic applications.
Steffen-Munsberg et al. (2015)
3 more

1 mention without citation

Structural characterization of the Mycobacterium tuberculosis biotin biosynthesis enzymes 7,8-diaminopelargonic acid synthase and dethiobiotin synthetase .
Dey et al. (2010)