3vk3

Crystal Structure of L-Methionine gamma-Lyase from Pseudomonas putida C116H Mutant Complexed with L-methionine

spinqualitylabelsall models 3vk3, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3vk3 is a 4 chain structure with sequence from Pseudomonas putida. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: LLP, MET Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MEGL_PSEPU Publication Abstract from PubMed Cys116, Lys240<sup>*</sup>, and Asp241<sup>*</sup> (asterisks indicate residues from the second subunit of the active dimer) at the active site of L-methionine gamma-lyase of Pseudomonas putida (MGL_Pp) are highly conserved among heterologous MGLs. In a previous study, we found that substitution of Cys116 for His led to a drastic increase in activity toward L-cysteine and a decrease in that toward L-methionine. In this study, we examined some properties of the C116H mutant by kinetic analysis and 3D structural analysis. We assumed that substitution of Cys116 for His broke the original hydrogen-bond network and that this induced a significant effect of Tyr114 as a general acid catalyst, possibly due to the narrow space in the active site. The C116H mutant acquired a novel beta-elimination activity and lead a drastic conformation change in the histidine residue at position 116 by binding the substrate, suggesting that this His residue affects the reaction specificity of C116H. Furthermore, we suggest that Lys240<sup>*</sup> is important for substrate recognition and structural stability and that Asp241<sup>*</sup> is also involved in substrate specificity in the elimination reaction. Based on this, we suggest that the hydrogen-bond network among Cys116, Lys240<sup>*</sup>, and Asp241<sup>*</sup> contributes to substrate specificity that is, to L-methionine recognition at the active site in MGL_Pp. The Role of Amino Acid Residues in the Active Site of <small>L</small>-Methionine gamma-lyase from <i>Pseudomonas putida</i>.,Fukumoto M, Kudou D, Murano S, Shiba T, Sato D, Tamura T, Harada S, Inagaki K Biosci Biotechnol Biochem. 2012 Jul 23;76(7):1275-84. Epub 2012 Jul 7. PMID:22785484 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Methionine gamma-lyase 3D structures

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