6JCM
Crystal structure of ligand-free Rv0187.
Summary for 6JCM
| Entry DOI | 10.2210/pdb6jcm/pdb |
| Descriptor | Probable O-methyltransferase, ACETATE ION (3 entities in total) |
| Functional Keywords | o-methyltransferase, mtb, comt, rossmann, transferase |
| Biological source | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| Total number of polymer chains | 4 |
| Total formula weight | 104774.40 |
| Authors | |
| Primary citation | Lee, S.,Kang, J.,Kim, J. Structural and biochemical characterization of Rv0187, an O-methyltransferase from Mycobacterium tuberculosis. Sci Rep, 9:8059-8059, 2019 Cited by PubMed Abstract: 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. PubMed: 31147608DOI: 10.1038/s41598-019-44592-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.08 Å) |
Structure validation
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