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B6db references: 10965031

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)
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

B6db references