3i5u
From Proteopedia
(Difference between revisions)
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3i5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i5u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3i5u RCSB], [http://www.ebi.ac.uk/pdbsum/3i5u PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3i5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i5u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3i5u RCSB], [http://www.ebi.ac.uk/pdbsum/3i5u PDBsum]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/Q84HC8_STRCZ Q84HC8_STRCZ]] S-adenosyl-L-methionine-dependent O-methyltransferase that catalyzes regiospecific methylation at the 7-hydroxy group of 2,7-dihydroxy-5-methyl-1-naphthoate in the biosynthesis of the naphthoate moiety of the neocarzinostatin chromophore. Also recognizes other dihydroxynaphthoate as substrates and catalyzes their regiospecific O-methylation. The carboxylate and its ortho-hydroxy groups of the substrate appear to be crucial for NcsB1 substrate recognition and binding, and O-methylation takes place only at the free hydroxy group of these dihydroxynaphthoic acids.<ref>PMID:18387946</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] |
Revision as of 21:55, 25 December 2014
Crystal structure of an O-methyltransferase (NcsB1) from neocarzinostatin biosynthesis in complex with S-adenosylmethionine (SAM) and 2-hydroxy-5-methyl naphthoic acid (MNA)
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