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PDBsum entry 2o7c
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References listed in PDB file
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Key reference
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Title
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Structure of the antitumour enzyme l-Methionine gamma-Lyase from pseudomonas putida at 1.8 a resolution.
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Authors
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D.Kudou,
S.Misaki,
M.Yamashita,
T.Tamura,
T.Takakura,
T.Yoshioka,
S.Yagi,
R.M.Hoffman,
A.Takimoto,
N.Esaki,
K.Inagaki.
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Ref.
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J Biochem (tokyo), 2007,
141,
535-544.
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PubMed id
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Abstract
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l-Methionine gamma-lyase (EC 4.4.1.11, MGL_Pp) from Pseudomonas putida is a
multifunctional enzyme, which belongs to the gamma-family of
pyridoxal-5'-phosphate (PLP) dependent enzymes. In this report, we demonstrate
that the three-dimensional structure of MGL_Pp has been completely solved by the
molecular replacement method to an R-factor of 20.4% at 1.8 A resolution.
Detailed information of the overall structure of MGL_Pp supplies a clear picture
of the substrate- and PLP-binding pockets. Tyr59 and Arg61 of neighbouring
subunits, which are strongly conserved in other gamma-family enzymes, contact
the phosphate group of PLP. These residues are important as the main anchor
within the active site. Lys240, Asp241 and Arg61 of one partner monomer and
Tyr114 and Cys116 of the other partner monomer form a hydrogen-bond network in
the MGL active site which is specific for MGLs. It is also suggested that
electrostatic interactions at the subunit interface are involved in the
stabilization of the structural conformation. The detailed structure will
facilitate the development of MGL_Pp as an anticancer drug.
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