5jr3: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5jr3]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_peucetius Streptomyces peucetius]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5JR3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5jr3]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_peucetius Streptomyces peucetius]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5JR3 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.84Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5jr3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jr3 OCA], [https://pdbe.org/5jr3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jr3 RCSB], [https://www.ebi.ac.uk/pdbsum/5jr3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jr3 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=5jr3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jr3 OCA], [https://pdbe.org/5jr3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jr3 RCSB], [https://www.ebi.ac.uk/pdbsum/5jr3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jr3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 12:14, 25 October 2023
Crystal structure of carminomycin-4-O-methyltransferase DnrK in complex with SAH and 4-methylumbelliferoneCrystal structure of carminomycin-4-O-methyltransferase DnrK in complex with SAH and 4-methylumbelliferone
Structural highlights
FunctionDNRK_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.[1] References
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