3ppc | pdb_00003ppc

Crystal structure of the Candida albicans methionine synthase by surface entropy reduction, tyrosine variant with zinc

spinqualitylabelsall models 3ppc, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ppc is a 2 chain structure with sequence from Candida albicans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: CL, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function METE_CANAL Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.[HAMAP-Rule:MF_00172] Publication Abstract from PubMed Fungal methionine synthase, Met6p, transfers a methyl group from 5-methyl-tetrahydrofolate to homocysteine to generate methionine. The enzyme is essential to fungal growth and is a potential anti-fungal drug design target. We have characterized the enzyme from the pathogen Candida albicans but were unable to crystallize it in native form. We converted Lys103, Lys104, and Glu107 all to Tyr (Met6pY), Thr (Met6pT) and Ala (Met6pA). All variants showed wild-type kinetic activity and formed useful crystals, each with unique crystal packing. In each case the mutated residues participated in beneficial crystal contacts. We have solved the three structures at 2.0-2.8A resolution and analyzed crystal packing, active-site residues, and similarity to other known methionine synthase structures. C. albicans Met6p has a two domain structure with each of the domains having a (betaalpha)(8)-barrel fold. The barrels are arranged face-to-face and the active site is located in a cleft between the two domains. Met6p utilizes a zinc ion for catalysis that is bound in the C-terminal domain and ligated by four conserved residues: His657, Cys659, Glu679 and Cys739. Structure of Candida albicans methionine synthase determined by employing surface residue mutagenesis.,Ubhi D, Kavanagh KL, Monzingo AF, Robertus JD Arch Biochem Biophys. 2011 Sep 1;513(1):19-26. doi:, 10.1016/j.abb.2011.06.002. Epub 2011 Jun 12. PMID:21689631 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Methionine synthase 3D structures

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