5jr3: Difference between revisions

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<StructureSection load='5jr3' size='340' side='right' caption='[[5jr3]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
<StructureSection load='5jr3' size='340' side='right' caption='[[5jr3]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
== Structural highlights ==
== 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>
<table><tr><td colspan='2'>[[5jr3]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/As_4.1799 As 4.1799]. 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>
</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dnrK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1950 AS 4.1799])</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>
<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>
<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>
<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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jr3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: As 4 1799]]
[[Category: Carminomycin 4-O-methyltransferase]]
[[Category: Carminomycin 4-O-methyltransferase]]
[[Category: Huber, T D]]
[[Category: Huber, T D]]

Revision as of 21:02, 15 November 2017

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

5jr3 is a 3 chain structure with sequence from As 4.1799. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Gene:dnrK (AS 4.1799)
Activity:Carminomycin 4-O-methyltransferase, with EC number 2.1.1.292
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.[1]

References

  1. ↑ Jansson A, Koskiniemi H, Mantsala P, Niemi J, Schneider G. Crystal structure of a ternary complex of DnrK, a methyltransferase in daunorubicin biosynthesis, with bound products. J Biol Chem. 2004 Sep 24;279(39):41149-56. Epub 2004 Jul 24. PMID:15273252 doi:10.1074/jbc.M407081200

5jr3, resolution 1.84Å

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