5jr3: Difference between revisions
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==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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Proteopedia Page Contributors and Editors (what is this?)
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
