View source for 6jcm


==Crystal structure of ligand-free Rv0187.==
<StructureSection load='6jcm' size='340' side='right'caption='[[6jcm]], [[Resolution|resolution]] 2.08&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6jcm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JCM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JCM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.08&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6jcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jcm OCA], [https://pdbe.org/6jcm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jcm RCSB], [https://www.ebi.ac.uk/pdbsum/6jcm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jcm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CAMT_MYCTU CAMT_MYCTU] Catechol O-methyltransferase that can use various catechol-like compounds such as gallic acid (GA), 3,4-dihydroxy-5-methoxy-benzoic acid (5OMeBA), protocatechuic acid (PCA), 3,4-dihydroxy-benzaldehyde (DHA), dopamine, caffeic acid (CA), luteolin, quercetin, and 5-hydroxyuridine.<ref>PMID:31147608</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

Structural and biochemical characterization of Rv0187, an O-methyltransferase from Mycobacterium tuberculosis.,Lee S, Kang J, Kim J Sci Rep. 2019 May 30;9(1):8059. doi: 10.1038/s41598-019-44592-7. PMID:31147608<ref>PMID:31147608</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6jcm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Kim J]]
[[Category: Lee S]]