› 6s0c

X-ray diffraction
1.46Å resolution

Crystal structure of methionine gamma-lyase from Citrobacter freundii modified by dimethylthiosulfinate

Released:
DOI: 10.2210/pdb6s0c/pdb
PDB entry 6s0c coloured by chain, front view.
PDB entry 6s0c coloured by chain, side view.
PDB entry 6s0c coloured by chain, top view.
Source organism: Citrobacter freundii
Primary publication:
Sulfoxides of sulfur-containing amino acids are suicide substrates of Citrobacter freundii methionine γ-lyase. Structural bases of the enzyme inactivation.
Revtovich S, Morozova E, Kulikova V, Koval V, Anufrieva N, Nikulin A, Demidkina T
Biochimie 168 190-197 (2020)
PMID: 31711941

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-100816 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-methionine gamma-lyase Chain: A
Molecule details ›
Chain: A
Length: 398 amino acids
Theoretical weight: 43.08 KDa
Source organism: Citrobacter freundii
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: A0A0A5P8W7 (Residues: 1-398; Coverage: 100%)
Gene names: AI2602V1_0214, AI2935V1_0207, AN672_11005, HV333_01080, HXS83_00935, I9Y29_001146, JDY53_20795, KV121_003196, KY227_003757, TO64_18625, megL
Sequence domains: Cys/Met metabolism PLP-dependent enzyme

Ligands and Environments


Cofactor: Ligand PLP 1 x PLP
1 bound ligand:
Ligand PGE 1 x PGE
1 modified residue:
Ligand SCH 3 x SCH

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: I222
Unit cell:
a: 56.784Å b: 123.255Å c: 128.328Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.138 0.137 0.172
Expression system: Escherichia coli K-12

Quick links

Citations

1 mention without citation

Structural Basis of the Inhibition of L-Methionine γ-Lyase from Fusobacterium nucleatum.
Bu et al. (2023)