3lcc | pdb_00003lcc

Structure of a SAM-dependent halide methyltransferase from Arabidopsis thaliana

spinqualitylabelsall models 3lcc, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3lcc is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: CL, SAH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HOL1_ARATH S-adenosyl-L-methionine-dependent methyltransferase. Involved in glucosinolate metabolism and defense against phytopathogens. Highly reactive to thiocyanate (NCS(-)) derived from myrosinase-mediated hydrolysis of glucosinolates upon tissue damage.[REFERENCE:8] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed A product structure of the halomethane producing enzyme in plants (Arabidopsis thaliana) is reported and a model for presentation of chloride/bromide ion to the methyl group of S-adenosyl-L-methionine (SAM) is presented to rationalise nucleophilic halide attack for halomethane production, gaseous natural products that are produced globally. Halomethane biosynthesis: structure of a SAM-dependent halide methyltransferase from Arabidopsis thaliana.,Schmidberger JW, James AB, Edwards R, Naismith JH, O'Hagan D Angew Chem Int Ed Engl. 2010 May 10;49(21):3646-8. doi: 10.1002/anie.201000119. PMID:20376845 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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