7oy1
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7oy1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_peucetius Streptomyces peucetius], [https://en.wikipedia.org/wiki/Streptomyces_purpurascens Streptomyces purpurascens], [https://en.wikipedia.org/wiki/Streptomyces_sp._ZEA17I Streptomyces sp. ZEA17I] 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=7OY1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OY1 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7oy1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_peucetius Streptomyces peucetius], [https://en.wikipedia.org/wiki/Streptomyces_purpurascens Streptomyces purpurascens], [https://en.wikipedia.org/wiki/Streptomyces_sp._ZEA17I Streptomyces sp. ZEA17I] 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=7OY1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OY1 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3VL:METHYL+(1R,2R,4S)-2-ETHYL-2,5,7-TRIHYDROXY-6,11-DIOXO-4-{[2,3,6-TRIDEOXY-3-(DIMETHYLAMINO)-ALPHA-L-LYXO-HEXOPYRANOSYL]OXY}-1,2,3,4,6,11-HEXAHYDROTETRACENE-1-CARBOXYLATE'>3VL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></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]] 2.39Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3VL:METHYL+(1R,2R,4S)-2-ETHYL-2,5,7-TRIHYDROXY-6,11-DIOXO-4-{[2,3,6-TRIDEOXY-3-(DIMETHYLAMINO)-ALPHA-L-LYXO-HEXOPYRANOSYL]OXY}-1,2,3,4,6,11-HEXAHYDROTETRACENE-1-CARBOXYLATE'>3VL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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=7oy1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oy1 OCA], [https://pdbe.org/7oy1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oy1 RCSB], [https://www.ebi.ac.uk/pdbsum/7oy1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oy1 ProSAT]</span></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=7oy1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oy1 OCA], [https://pdbe.org/7oy1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oy1 RCSB], [https://www.ebi.ac.uk/pdbsum/7oy1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oy1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/A0A2V2Q0Q4_9ACTN A0A2V2Q0Q4_9ACTN] [https://www.uniprot.org/uniprot/I2N5E8_STRT9 I2N5E8_STRT9] [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/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 == | ||
<references/> | <references/> | ||
Current revision
DnrK mutant RTCR
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