7pga
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==Chimeric carminomycin-4-O-methyltransferase (DnrK) with regions from 10-hydroxylase RdmB and 10-decarboxylase TamK== | ==Chimeric carminomycin-4-O-methyltransferase (DnrK) with regions from 10-hydroxylase RdmB and 10-decarboxylase TamK== | ||
| - | <StructureSection load='7pga' size='340' side='right'caption='[[7pga]]' scene=''> | + | <StructureSection load='7pga' size='340' side='right'caption='[[7pga]], [[Resolution|resolution]] 2.77Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PGA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PGA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7pga]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_peucetius Streptomyces peucetius], [https://en.wikipedia.org/wiki/Streptomyces_purpurascens Streptomyces purpurascens] and [https://en.wikipedia.org/wiki/Streptomyces_tsukubensis_NRRL18488 Streptomyces tsukubensis NRRL18488]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PGA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PGA FirstGlance]. <br> |
| - | </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=7pga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pga OCA], [https://pdbe.org/7pga PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pga RCSB], [https://www.ebi.ac.uk/pdbsum/7pga PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pga ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.77Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=VAK:METHYL+(1R,2R,4S)-2-ETHYL-2,4,5,7-TETRAHYDROXY-6,11-DIOXO-1,2,3,4,6,11-HEXAHYDROTETRACENE-1-CARBOXYLATE'>VAK</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=7pga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pga OCA], [https://pdbe.org/7pga PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pga RCSB], [https://www.ebi.ac.uk/pdbsum/7pga PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pga ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/RDMB_STREF RDMB_STREF] Involved in the biosynthesis of the anthracycline aclacinomycin which is an aromatic polyketide antibiotic that exhibits high cytotoxicity and is widely applied in the chemotherapy of a variety of cancers. In vivo and in vitro, RdmB catalyzes the removal of the carboxylic group from the C-10 position of 15-demethoxyaclacinomycin T coupled to hydroxylation at the same C-10 position. It could also catalyze the removal of the carboxylic group at the C-10 position of 15-demethoxy-epsilon-rhodomycin coupled to hydroxylation at the same C-10 position to yield rhodomycin B. The reaction catalyzes by RdmB is intriguing, since the enzyme does not use any of the cofactors usually associated with hydroxylases such as flavins and/or metal ions to activate molecular oxygen.<ref>PMID:11004563</ref> <ref>PMID:15548527</ref> [https://www.uniprot.org/uniprot/I2N5E8_STRT9 I2N5E8_STRT9] [https://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__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Streptomyces peucetius]] | ||
| + | [[Category: Streptomyces purpurascens]] | ||
| + | [[Category: Streptomyces tsukubensis NRRL18488]] | ||
[[Category: Dinis P]] | [[Category: Dinis P]] | ||
[[Category: MetsaKetela M]] | [[Category: MetsaKetela M]] | ||
Current revision
Chimeric carminomycin-4-O-methyltransferase (DnrK) with regions from 10-hydroxylase RdmB and 10-decarboxylase TamK
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