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 language | English |
|---|---|
| Pages (from-to) | 349-354 |
| Number of pages | 6 |
| Journal | Journal of Biochemistry |
| Volume | 128 |
| Issue number | 3 |
| Publication status | Published - 2000 |
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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 journal › Article
}
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 -