5jr3
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of carminomycin-4-O-methyltransferase DnrK in complex with SAH and 4-methylumbelliferone== | |
- | + | <StructureSection load='5jr3' size='340' side='right' caption='[[5jr3]], [[Resolution|resolution]] 1.84Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[5jr3]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JR3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JR3 FirstGlance]. <br> | |
- | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4MU:7-HYDROXY-4-METHYL-2H-CHROMEN-2-ONE'>4MU</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |
- | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carminomycin_4-O-methyltransferase Carminomycin 4-O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.292 2.1.1.292] </span></td></tr> | |
- | [[Category: | + | <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=5jr3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jr3 OCA], [http://pdbe.org/5jr3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jr3 RCSB], [http://www.ebi.ac.uk/pdbsum/5jr3 PDBsum]</span></td></tr> |
- | [[Category: Huber, T | + | </table> |
- | [[Category: | + | == Function == |
- | [[Category: Enzyme Discovery | + | [[http://www.uniprot.org/uniprot/DNRK_STRPE DNRK_STRPE]] Involved in the biosynthesis of the anthracyclines carminomycin and daunorubicin (daunomycin) which are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. In vivo, catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to the 4-O-position of carminomycin to form daunorubicin. In vitro, it also methylates the anthracyclines rhodomycin D (10-carbomethoxy-13-deoxycarminomycin) and 13-deoxy-carminomycin at the 4-hydroxyl position. It is quite specific with respect to the length of the carbohydrate chain at the C7 position, but it can accept substrates with bulky substituent at C10 position.<ref>PMID:15273252</ref> |
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Carminomycin 4-O-methyltransferase]] | ||
+ | [[Category: Huber, T D]] | ||
+ | [[Category: Johnson, B R]] | ||
+ | [[Category: NatPro, Enzyme Discovery for Natural Product Biosynthesis]] | ||
+ | [[Category: Phillips, G N]] | ||
[[Category: Singh, S]] | [[Category: Singh, S]] | ||
- | [[Category: | + | [[Category: Thorson, J S]] |
- | [[Category: | + | [[Category: Wang, F]] |
+ | [[Category: Enzyme discovery for natural product biosynthesis]] | ||
+ | [[Category: Natpro]] | ||
+ | [[Category: Natural product biosynthesis]] | ||
+ | [[Category: PSI, Protein structure initiative]] | ||
+ | [[Category: Psi-biology]] | ||
+ | [[Category: Structural genomic]] | ||
+ | [[Category: Transferase]] |
Revision as of 06:11, 2 June 2016
Crystal structure of carminomycin-4-O-methyltransferase DnrK in complex with SAH and 4-methylumbelliferone
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Categories: Carminomycin 4-O-methyltransferase | Huber, T D | Johnson, B R | NatPro, Enzyme Discovery for Natural Product Biosynthesis | Phillips, G N | Singh, S | Thorson, J S | Wang, F | Enzyme discovery for natural product biosynthesis | Natpro | Natural product biosynthesis | PSI, Protein structure initiative | Psi-biology | Structural genomic | Transferase