Crystal structure of the pyridoxal 5'-phosphate dependent L-methionine γ-lyase from Pseudomonas putida

Hiroyuki Motoshima, Kenji Inagaki, Takashi Kumasaka, Makio Furuichi, Hiroyuki Inoue, Takashi Tamura, Nobuyoshi Esaki, Kenji Soda, Nobuo Tanaka, Masaki Yamamoto, Hidehiko Tanaka

Research output: Contribution to journalArticlepeer-review

46 Citations (Scopus)

Abstract

L-Methionine γ-lyase (MGL) catalyzes the pyridoxal 5'-phosphate (PLP) dependent α,γ-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∅ 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 β-lyase and L-cystathionine γ-synthase from Escherichia coli.

Original languageEnglish
Pages (from-to)349-354
Number of pages6
JournalJournal of biochemistry
Volume128
Issue number3
DOIs
Publication statusPublished - 2000

Keywords

  • Crystal structure
  • L-methionine γ-lyase
  • MAD
  • PLP enzyme
  • Pseudomonas putida

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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