› 4u1t

X-ray diffraction
2Å resolution

The crystal structure of holo CalE6, a methionine gamma lyase from Micromonospora echinospora

Released:
DOI: 10.2210/pdb4u1t/pdb
PDB entry 4u1t coloured by chain, front view.
PDB entry 4u1t coloured by chain, side view.
PDB entry 4u1t coloured by chain, top view.
Source organism: Micromonospora echinospora
Primary publication:
Identification and characterization of a methionine γ-lyase in the calicheamicin biosynthetic cluster of Micromonospora echinospora.
Song H, Xu R, Guo Z
Chembiochem 16 100-9 (2015)
PMID: 25404066

Function and Biology Details

Reaction catalysed: 
(1a) L-methionine = methanethiol + 2-aminobut-2-enoate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185189 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cystathionine gamma-synthase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 389 amino acids
Theoretical weight: 41.98 KDa
Source organism: Micromonospora echinospora
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8KNG3 (Residues: 1-381; Coverage: 100%)
Gene name: calE6
Sequence domains: Cys/Met metabolism PLP-dependent enzyme
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 8 x SO4
1 modified residue:
Ligand LLP 8 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: I222
Unit cell:
a: 146.17Å b: 146.22Å c: 348.091Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.153 0.152 0.184
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Pyridoxal phosphate-dependent reactions in the biosynthesis of natural products.
Du et al. (2019)
1 more

1 mention without citation

Structural dynamics of a methionine γ-lyase for calicheamicin biosynthesis: Rotation of the conserved tyrosine stacking with pyridoxal phosphate.
Cao et al. (2016)