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

H. Motoshima, Kenji Inagaki, T. Kumasaka, M. Furuichi, H. Inoue, Takashi Tamura, N. Esaki, K. Soda, N. Tanaka, M. Yamamoto, H. Tanaka

Research output: Contribution to journalArticle

45 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
Publication statusPublished - 2000

Fingerprint

Cystathionine
Pseudomonas putida
Lyases
Pyridoxal Phosphate
Methionine
R388
Diffraction
Crystal structure
Synchrotrons
Synchrotron radiation
Dimers
Escherichia coli
Monomers
Radiation

Keywords

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

ASJC Scopus subject areas

  • Biochemistry

Cite this

Crystal structure of the pyridoxal 5'-phosphate dependent L-methionine γ-lyase from Pseudomonas putida. / Motoshima, H.; Inagaki, Kenji; Kumasaka, T.; Furuichi, M.; Inoue, H.; Tamura, Takashi; Esaki, N.; Soda, K.; Tanaka, N.; Yamamoto, M.; Tanaka, H.

In: Journal of Biochemistry, Vol. 128, No. 3, 2000, p. 349-354.

Research output: Contribution to journalArticle

Motoshima, H, Inagaki, K, Kumasaka, T, Furuichi, M, Inoue, H, Tamura, T, Esaki, N, Soda, K, Tanaka, N, Yamamoto, M & Tanaka, H 2000, 'Crystal structure of the pyridoxal 5'-phosphate dependent L-methionine γ-lyase from Pseudomonas putida', Journal of Biochemistry, vol. 128, no. 3, pp. 349-354.
Motoshima, H. ; Inagaki, Kenji ; Kumasaka, T. ; Furuichi, M. ; Inoue, H. ; Tamura, Takashi ; Esaki, N. ; Soda, K. ; Tanaka, N. ; Yamamoto, M. ; Tanaka, H. / Crystal structure of the pyridoxal 5'-phosphate dependent L-methionine γ-lyase from Pseudomonas putida. In: Journal of Biochemistry. 2000 ; Vol. 128, No. 3. pp. 349-354.
@article{e4ec9e2bc56e450092cd1977240c6725,
title = "Crystal structure of the pyridoxal 5'-phosphate dependent L-methionine γ-lyase from Pseudomonas putida",
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.",
keywords = "Crystal structure, L-methionine γ-lyase, MAD, PLP enzyme, Pseudomonas putida",
author = "H. Motoshima and Kenji Inagaki and T. Kumasaka and M. Furuichi and H. Inoue and Takashi Tamura and N. Esaki and K. Soda and N. Tanaka and M. Yamamoto and H. Tanaka",
year = "2000",
language = "English",
volume = "128",
pages = "349--354",
journal = "Journal of Biochemistry",
issn = "0021-924X",
publisher = "Oxford University Press",
number = "3",

}

TY - JOUR

T1 - Crystal structure of the pyridoxal 5'-phosphate dependent L-methionine γ-lyase from Pseudomonas putida

AU - Motoshima, H.

AU - Inagaki, Kenji

AU - Kumasaka, T.

AU - Furuichi, M.

AU - Inoue, H.

AU - Tamura, Takashi

AU - Esaki, N.

AU - Soda, K.

AU - Tanaka, N.

AU - Yamamoto, M.

AU - Tanaka, H.

PY - 2000

Y1 - 2000

N2 - 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.

AB - 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.

KW - Crystal structure

KW - L-methionine γ-lyase

KW - MAD

KW - PLP enzyme

KW - Pseudomonas putida

UR - http://www.scopus.com/inward/record.url?scp=0033809243&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033809243&partnerID=8YFLogxK

M3 - Article

C2 - 10965031

AN - SCOPUS:0033809243

VL - 128

SP - 349

EP - 354

JO - Journal of Biochemistry

JF - Journal of Biochemistry

SN - 0021-924X

IS - 3

ER -