› 3asb

X-ray diffraction
2.7Å resolution

Crystal structure of PLP-bound LL-diaminopimelate aminotransferase from Chlamydia trachomatis

Released:
DOI: 10.2210/pdb3asb/pdb
PDB entry 3asb coloured by chain, front view.
PDB entry 3asb coloured by chain, side view.
PDB entry 3asb coloured by chain, top view.
Source organism: Chlamydia trachomatis
Primary publication:
The structure of LL-diaminopimelate aminotransferase from Chlamydia trachomatis: implications for its broad substrate specificity.
Watanabe N, Clay MD, van Belkum MJ, Fan C, Vederas JC, James MN
J Mol Biol 411 649-60 (2011)
PMID: 21722650

Function and Biology Details

Reaction catalysed: 
LL-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131406 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
LL-diaminopimelate aminotransferase Chain: A
Molecule details ›
Chain: A
Length: 400 amino acids
Theoretical weight: 44.94 KDa
Source organism: Chlamydia trachomatis
Expression system: Escherichia coli
UniProt:
  • Canonical: O84395 (Residues: 1-394; Coverage: 100%)
Gene names: CT_390, aspC, dapL
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand LLP 1 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: I4122
Unit cell:
a: 110.486Å b: 110.486Å c: 204.242Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.225 0.222 0.287
Expression system: Escherichia coli

Quick links

Citations

6 citation in other articles

Genomic and Biochemical Analysis of the Diaminopimelate and Lysine Biosynthesis Pathway in Verrucomicrobium spinosum: Identification and Partial Characterization of L,L-Diaminopimelate Aminotransferase and UDP-N-Acetylmuramoylalanyl-D-glutamyl-2,6-meso-Diaminopimelate Ligase.
Nachar et al. (2012)
5 more

1 mention without citation

Structure of ALD1, a plant-specific homologue of the universal diaminopimelate aminotransferase enzyme of lysine biosynthesis.
Sobolev et al. (2013)