1gc2
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CRYSTAL STRUCTURE OF THE PYRIDOXAL-5'-PHOSPHATE DEPENDENT L-METHIONINE GAMMA-LYASE FROM PSEUDOMONAS PUTIDA
OverviewOverview
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.
About this StructureAbout this Structure
1GC2 is a Single protein structure of sequence from Pseudomonas putida. Active as Methionine gamma-lyase, with EC number 4.4.1.11 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the pyridoxal 5'-phosphate dependent L-methionine gamma-lyase from Pseudomonas putida., Motoshima H, Inagaki K, Kumasaka T, Furuichi M, Inoue H, Tamura T, Esaki N, Soda K, Tanaka N, Yamamoto M, Tanaka H, J Biochem. 2000 Sep;128(3):349-54. PMID:10965031
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