3i5u

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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>
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== Function ==
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[[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)

3i5u, resolution 2.60Å

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