Crystal structure of the pyridoxal 5'-phosphate dependent L-methionine gamma-lyase from Pseudomonas putida.
L-Methionine gamma-lyase (MGL) catalyzes the pyridoxal 5'-phosphate (PLP) dependent alpha,gamma-elimination of L-methionine. We have determined two crystal structures of MGL from Pseudomonas putida using MAD (multiwavelength anomalous diffraction) and molecular replacement methods. The structures have been refined to an R-factor of 21.1% at 2.0 and 1.7 A resolution using synchrotron radiation diffraction data. A homotetramer with 222 symmetry is built up by non-crystallographic symmetry. Two monomers associate to build the active dimer. The spatial fold of subunits, with three functionally distinct domains and their quarternary arrangement, is similar to those of L-cystathionine beta-lyase and L-cystathionine gamma-synthase from Escherichia coli.
Motoshima
H
H
RIKEN Harima Institute, Kouto, Mikazuki, Sayo-gun, Hyogo 679-5148, Japan.
Inagaki
K
K
Kumasaka
T
T
Furuichi
M
M
Inoue
H
H
Tamura
T
T
Esaki
N
N
Soda
K
K
Tanaka
N
N
Yamamoto
M
M
Tanaka
H
H
D000595:Amino Acid Sequence; D001665:Binding Sites; D013437:Carbon-Sulfur Lyases / Q000737:chemistry* / Q000235:genetics; D018360:Crystallography, X-Ray; D008715:Methionine / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D016958:Pseudomonas putida / Q000201:enzymology*; D011732:Pyridoxal Phosphate / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D014961:X-Ray Diffraction
D011732:Pyridoxal Phosphate; D008715:Methionine; D013437:Carbon-Sulfur Lyases; C021558:L-methionine gamma-lyase