2O7C
Crystal structure of L-methionine-lyase from Pseudomonas
Summary for 2O7C
| Entry DOI | 10.2210/pdb2o7c/pdb |
| Descriptor | Methionine gamma-lyase, SULFATE ION (3 entities in total) |
| Functional Keywords | plp, methionine, cancer, lyase |
| Biological source | Pseudomonas putida |
| Total number of polymer chains | 4 |
| Total formula weight | 171991.19 |
| Authors | Misaki, S.,Takimoto, A.,Takakura, T.,Yoshioka, T.,Yamashita, M.,Tamura, T.,Tanaka, H.,Inagaki, K. (deposition date: 2006-12-10, release date: 2007-12-11, Last modification date: 2023-12-27) |
| Primary citation | Kudou, D.,Misaki, S.,Yamashita, M.,Tamura, T.,Takakura, T.,Yoshioka, T.,Yagi, S.,Hoffman, R.M.,Takimoto, A.,Esaki, N.,Inagaki, K. Structure of the antitumour enzyme L-methionine gamma-lyase from Pseudomonas putida at 1.8 A resolution J.Biochem.(Tokyo), 141:535-544, 2007 Cited by PubMed Abstract: 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. PubMed: 17289792DOI: 10.1093/jb/mvm055 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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