› 3oqv

X-ray diffraction
1.9Å resolution

AlbC, a cyclodipeptide synthase from Streptomyces noursei

Released:
DOI: 10.2210/pdb3oqv/pdb
Model geometry
Fit model/data
PDB entry 3oqv coloured by chain, front view.
PDB entry 3oqv coloured by chain, side view.
PDB entry 3oqv coloured by chain, top view.
Source organism: Streptomyces noursei
Primary publication:
Cyclodipeptide synthases, a family of class-I aminoacyl-tRNA synthetase-like enzymes involved in non-ribosomal peptide synthesis.
Sauguet L, Moutiez M, Li Y, Belin P, Seguin J, Le Du MH, Thai R, Masson C, Fonvielle M, Pernodet JL, Charbonnier JB, Gondry M
OpenAccess logo Nucleic Acids Res 39 4475-89 (2011)
PMID: 21296757

Function and Biology Details

Reaction catalysed: 
L-leucyl-tRNA(Leu) + L-phenylalanyl-tRNA(Phe) = tRNA(Leu) + tRNA(Phe) + cyclo(L-leucyl-L-phenylalanyl)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184500 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cyclo(L-leucyl-L-phenylalanyl) synthase Chain: A
Molecule details ›
Chain: A
Length: 247 amino acids
Theoretical weight: 27.81 KDa
Source organism: Streptomyces noursei
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8GED7 (Residues: 2-239; Coverage: 100%)
Gene name: albC
Sequence domains: Cyclodipeptide synthase
Structure domains: Cyclodipeptide synthase

Ligands and Environments

2 bound ligands:
Ligand DTD 1 x DTD
Ligand PO4 3 x PO4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: I4
Unit cell:
a: 97.17Å b: 97.17Å c: 45.46Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.186 0.236
Expression system: Escherichia coli

Quick links

Citations

15 review citations

tRNAs as regulators of biological processes.
Raina et al. (2014)
14 more

5 mentions without citation

The tRNA-dependent biosynthesis of modified cyclic dipeptides.
Giessen et al. (2014)
4 more