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Structural and biochemical characterization of Rv0187, an O-methyltransferase from Mycobacterium tuberculosis
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Structural and biochemical characterization of Rv0187, an O-methyltransferase from Mycobacterium tuberculosis
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Structural and biochemical characterization of Rv0187, an O-methyltransferase from Mycobacterium tuberculosis
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Journal Article
Structural and biochemical characterization of Rv0187, an O-methyltransferase from Mycobacterium tuberculosis
2019
Overview
Catechol O-methyltransferase (COMT) is widely distributed in nature and installs a methyl group onto one of the vicinal hydroxyl groups of a catechol derivative. Enzymes belonging to this family require two cofactors for methyl transfer: S-adenosyl-l-methionine as a methyl donor and a divalent metal cation for regiospecific binding and activation of a substrate. We have determined two high-resolution crystal structures of Rv0187, one of three COMT paralogs from
Mycobacterium tuberculosis
, in the presence and absence of cofactors. The cofactor-bound structure clearly locates strontium ions and S-adenosyl-l-homocysteine in the active site, and together with the complementary structure of the ligand-free form, it suggests conformational dynamics induced by the binding of cofactors. Examination of
in vitro
activities revealed promiscuous substrate specificity and relaxed regioselectivity against various catechol-like compounds. Unexpectedly, mutation of the proposed catalytic lysine residue did not abolish activity but altered the overall landscape of regiospecific methylation.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 82/16
/ 82/58
/ 82/83
/ Bacterial Proteins - genetics
/ Bacterial Proteins - isolation & purification
/ Bacterial Proteins - metabolism
/ Bacterial Proteins - ultrastructure
/ Catechol
/ Catechol O-methyltransferase
/ Catechol O-Methyltransferase - genetics
/ Catechol O-Methyltransferase - isolation & purification
/ Catechol O-Methyltransferase - metabolism
/ Catechol O-Methyltransferase - ultrastructure
/ Humanities and Social Sciences
/ Lysine
/ Mutation
/ Mycobacterium tuberculosis - enzymology
/ Mycobacterium tuberculosis - genetics
/ Recombinant Proteins - genetics
/ Recombinant Proteins - isolation & purification
/ Recombinant Proteins - metabolism
/ Recombinant Proteins - ultrastructure
/ S-Adenosylhomocysteine - metabolism
/ Science
