4wxh - Revision history

OCA at 10:45, 10 January 2024

2024-01-10T10:45:13Z

←Older revision		Revision as of 10:45, 10 January 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4wxh]] is a 2 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=4WXH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WXH FirstGlance]. <br>		<table><tr><td colspan='2'>[[4wxh]] is a 2 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=4WXH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WXH 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=DTU:(2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL'>DTU</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]] 1.9Å</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=DTU:(2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL'>DTU</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=4wxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxh OCA], [https://pdbe.org/4wxh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wxh RCSB], [https://www.ebi.ac.uk/pdbsum/4wxh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wxh 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=4wxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxh OCA], [https://pdbe.org/4wxh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wxh RCSB], [https://www.ebi.ac.uk/pdbsum/4wxh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wxh ProSAT]</span></td></tr>
	</table>		</table>

OCA at 21:01, 12 April 2023

2023-04-12T21:01:55Z

←Older revision		Revision as of 21:01, 12 April 2023
Line 1:		Line 1:

	==Carminomycin-4-O-methyltransferase (DnrK) variant (298Ser insert) in complex with S-adenosyl-L-homocysteine (SAH) and aclacinomycin T==		==Carminomycin-4-O-methyltransferase (DnrK) variant (298Ser insert) in complex with S-adenosyl-L-homocysteine (SAH) and aclacinomycin T==
-	<StructureSection load='4wxh' size='340' side='right' caption='[[4wxh]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='4wxh' size='340' side='right'caption='[[4wxh]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4wxh]] is a 2 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=4WXH OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4WXH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4wxh]] is a 2 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=4WXH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WXH FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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=DTU:(2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL'>DTU</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" 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=DTU:(2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL'>DTU</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1tw2\|1tw2]], [[1tw3\|1tw3]]</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=4wxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxh OCA], [https://pdbe.org/4wxh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wxh RCSB], [https://www.ebi.ac.uk/pdbsum/4wxh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wxh ProSAT]</span></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='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=4wxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxh OCA], [~~http~~://pdbe.org/4wxh PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4wxh RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4wxh PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4wxh ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[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>	+	[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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~As 4 1799~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Carminomycin 4-O-methyltransferase~~]]	+	[[Category: Streptomyces peucetius]]
-	[[Category: Metsa-Ketela, M]]	+	[[Category: Metsa-Ketela M]]
-	[[Category: Niiranen, L]]	+	[[Category: Niiranen L]]
-	~~[[Category: Antibiotic binding]]~~	+
-	~~[[Category: Methyltransferase]]~~	+
-	~~[[Category: Mono-oxygenase]]~~	+
-	~~[[Category: Sah binding]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 07:04, 28 February 2018

2018-02-28T07:04:17Z

←Older revision		Revision as of 07:04, 28 February 2018
Line 1:		Line 1:

-	==Carminomycin-4-O-methyltransferase (DnrK) variant (298Ser insert) in complex with S-adenosyl-L-~~homocystein~~ (SAH) and aclacinomycin T==	+	==Carminomycin-4-O-methyltransferase (DnrK) variant (298Ser insert) in complex with S-adenosyl-L-homocysteine (SAH) and aclacinomycin T==
	<StructureSection load='4wxh' size='340' side='right' caption='[[4wxh]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='4wxh' size='340' side='right' caption='[[4wxh]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4wxh]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WXH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WXH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4wxh]] is a 2 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=4WXH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WXH FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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=DTU:(2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL'>DTU</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=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=DTU:(2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL'>DTU</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1tw2\|1tw2]], [[1tw3\|1tw3]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1tw2\|1tw2]], [[1tw3\|1tw3]]</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=4wxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxh OCA], [http://pdbe.org/4wxh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wxh RCSB], [http://www.ebi.ac.uk/pdbsum/4wxh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wxh ProSAT]</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=4wxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxh OCA], [http://pdbe.org/4wxh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wxh RCSB], [http://www.ebi.ac.uk/pdbsum/4wxh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wxh ProSAT]</span></td></tr>
Line 24:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: As 4 1799]]
	[[Category: Carminomycin 4-O-methyltransferase]]		[[Category: Carminomycin 4-O-methyltransferase]]
	[[Category: Metsa-Ketela, M]]		[[Category: Metsa-Ketela, M]]

OCA at 14:11, 24 May 2017

2017-05-24T14:11:20Z

←Older revision		Revision as of 14:11, 24 May 2017
Line 1:		Line 1:
		+
	==Carminomycin-4-O-methyltransferase (DnrK) variant (298Ser insert) in complex with S-adenosyl-L-homocystein (SAH) and aclacinomycin T==		==Carminomycin-4-O-methyltransferase (DnrK) variant (298Ser insert) in complex with S-adenosyl-L-homocystein (SAH) and aclacinomycin T==
	<StructureSection load='4wxh' size='340' side='right' caption='[[4wxh]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='4wxh' size='340' side='right' caption='[[4wxh]], [[Resolution\|resolution]] 1.90Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1tw2\|1tw2]], [[1tw3\|1tw3]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1tw2\|1tw2]], [[1tw3\|1tw3]]</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=4wxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wxh RCSB], [http://www.ebi.ac.uk/pdbsum/4wxh 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=4wxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxh OCA], [http://pdbe.org/4wxh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wxh RCSB], [http://www.ebi.ac.uk/pdbsum/4wxh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wxh ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4wxh" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:20, 12 August 2015

2015-08-12T08:20:57Z

←Older revision		Revision as of 08:20, 12 August 2015
Line 10:		Line 10:
	== Function ==		== Function ==
	[[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>		[[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>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Bacterial secondary metabolic pathways are responsible for the biosynthesis of thousands of bioactive natural products. Many enzymes residing in these pathways have evolved to catalyze unusual chemical transformations, which is facilitated by an evolutionary pressure promoting chemical diversity. Such divergent enzyme evolution has been observed in S-adenosyl-l-methionine (SAM)-dependent methyltransferases involved in the biosynthesis of anthracycline anticancer antibiotics; whereas DnrK from the daunorubicin pathway is a canonical 4-O-methyltransferase, the closely related RdmB (52% sequence identity) from the rhodomycin pathways is an atypical 10-hydroxylase that requires SAM, a thiol reducing agent, and molecular oxygen for activity. Here, we have used extensive chimeragenesis to gain insight into the functional differentiation of RdmB and show that insertion of a single serine residue to DnrK is sufficient for introduction of the monooxygenation activity. The crystal structure of DnrK-Ser in complex with aclacinomycin T and S-adenosyl-l-homocysteine refined to 1.9-A resolution revealed that the inserted serine S297 resides in an alpha-helical segment adjacent to the substrate, but in a manner where the side chain points away from the active site. Further experimental work indicated that the shift in activity is mediated by rotation of a preceding phenylalanine F296 toward the active site, which blocks a channel to the surface of the protein that is present in native DnrK. The channel is also closed in RdmB and may be important for monooxygenation in a solvent-free environment. Finally, we postulate that the hydroxylation ability of RdmB originates from a previously undetected 10-decarboxylation activity of DnrK.
		+
		+	Divergent evolution of an atypical S-adenosyl-l-methionine-dependent monooxygenase involved in anthracycline biosynthesis.,Grocholski T, Dinis P, Niiranen L, Niemi J, Metsa-Ketela M Proc Natl Acad Sci U S A. 2015 Jul 27. pii: 201501765. PMID:26216966<ref>PMID:26216966</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 14:50, 29 July 2015

2015-07-29T14:50:15Z

←Older revision		Revision as of 14:50, 29 July 2015
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-	'''~~Unreleased structure~~'''	+	==Carminomycin-4-O-methyltransferase (DnrK) variant (298Ser insert) in complex with S-adenosyl-L-homocystein (SAH) and aclacinomycin T==
-		+	<StructureSection load='4wxh' size='340' side='right' caption='[[4wxh]], [[Resolution\|resolution]] 1.90Å' scene=''>
-	~~The entry~~ 4wxh is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4wxh]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WXH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WXH FirstGlance]. <br>
-	~~Authors~~: ~~Metsa~~-~~Ketela~~, M., ~~Niiranen~~, L.	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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=DTU:(2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL'>DTU</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1tw2\|1tw2]], [[1tw3\|1tw3]]</td></tr>
-	~~Description~~: ~~Carminomycin~~-4-O-methyltransferase (~~DnrK) variant (298Ser insert~~) in ~~complex with~~ S-adenosyl-L-~~homocystein~~ (~~SAH~~) and ~~aclacinomycin T~~	+	<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: ~~Unreleased Structures~~]]	+	<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=4wxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wxh RCSB], [http://www.ebi.ac.uk/pdbsum/4wxh PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[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: Metsa-Ketela, M]]		[[Category: Metsa-Ketela, M]]
	[[Category: Niiranen, L]]		[[Category: Niiranen, L]]
		+	[[Category: Antibiotic binding]]
		+	[[Category: Methyltransferase]]
		+	[[Category: Mono-oxygenase]]
		+	[[Category: Sah binding]]
		+	[[Category: Transferase]]

OCA at 20:09, 24 December 2014

2014-12-24T20:09:55Z

←Older revision		Revision as of 20:09, 24 December 2014
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	Description: Carminomycin-4-O-methyltransferase (DnrK) variant (298Ser insert) in complex with S-adenosyl-L-homocystein (SAH) and aclacinomycin T		Description: Carminomycin-4-O-methyltransferase (DnrK) variant (298Ser insert) in complex with S-adenosyl-L-homocystein (SAH) and aclacinomycin T
		+	[[Category: Unreleased Structures]]
		+	[[Category: Metsa-Ketela, M]]
		+	[[Category: Niiranen, L]]

OCA at 08:41, 3 December 2014

2014-12-03T08:41:14Z

←Older revision		Revision as of 08:41, 3 December 2014
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4wxh is ON HOLD	+	The entry 4wxh is ON HOLD until Paper Publication

	Authors: Metsa-Ketela, M., Niiranen, L.		Authors: Metsa-Ketela, M., Niiranen, L.

	Description: Carminomycin-4-O-methyltransferase (DnrK) variant (298Ser insert) in complex with S-adenosyl-L-homocystein (SAH) and aclacinomycin T		Description: Carminomycin-4-O-methyltransferase (DnrK) variant (298Ser insert) in complex with S-adenosyl-L-homocystein (SAH) and aclacinomycin T

OCA: Protected "4wxh" [edit=sysop:move=sysop]

2014-11-19T12:02:40Z

Protected "4wxh" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:02, 19 November 2014

OCA: New page: '''Unreleased structure''' The entry 4wxh is ON HOLD Authors: Metsa-Ketela, M., Niiranen, L. Description: Carminomycin-4-O-methyltransferase (DnrK) variant (298Ser insert) in complex w...

2014-11-19T12:02:39Z

New page: '''Unreleased structure''' The entry 4wxh is ON HOLD Authors: Metsa-Ketela, M., Niiranen, L. Description: Carminomycin-4-O-methyltransferase (DnrK) variant (298Ser insert) in complex w...

New page

'''Unreleased structure'''

The entry 4wxh is ON HOLD

Authors: Metsa-Ketela, M., Niiranen, L.

Description: Carminomycin-4-O-methyltransferase (DnrK) variant (298Ser insert) in complex with S-adenosyl-L-homocystein (SAH) and aclacinomycin T