|
type |
Journal Article |
authors |
Motoshima, H.; Inagaki, K.; Kumasaka, T.; Furuichi, M.; Inoue, H.; Tamura, T.; Esaki, N.; Soda, K.; Tanaka, N.; Yamamoto, M.; Tanaka, H. |
title |
Crystal structure of the pyridoxal 5'-phosphate dependent L-methionine gamma-lyase from Pseudomonas putida |
journal |
J Biochem (Tokyo) |
Activity |
4.4.1.11 |
sel |
selected |
ui |
10965031 |
year |
(2000) |
volume |
128 |
number |
3 |
pages |
349-54 |
| |
keywords |
Amino Acid Sequence |
abstract |
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. |
last changed |
2009/07/01 14:07 |
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