3lcc
From Proteopedia
Structure of a SAM-dependent halide methyltransferase from Arabidopsis thaliana
Structural highlights
FunctionHOL1_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][1] 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 PubMedA 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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