2erc - Revision history

OCA at 09:19, 14 February 2024

2024-02-14T09:19:23Z

← Older revision		Revision as of 09:19, 14 February 2024
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	<StructureSection load='2erc' size='340' side='right'caption='[[2erc]], [[Resolution\|resolution]] 3.03Å' scene=''>		<StructureSection load='2erc' size='340' side='right'caption='[[2erc]], [[Resolution\|resolution]] 3.03Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2erc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"vibrio_subtilis"_ehrenberg_1835 "vibrio~~ subtilis~~" ehrenberg 1835~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ERC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ERC FirstGlance]. <br>		<table><tr><td colspan='2'>[[2erc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ERC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ERC FirstGlance]. <br>
	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>ERMC' ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~1423~~ "~~Vibrio subtilis~~" ~~Ehrenberg 1835])</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]] 3.03Å</td></tr>
	~~<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'~~>[~~https://en.wikipedia.org/wiki/Transferase Transferase~~]~~, with EC number [https://www~~.~~brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.181, 2.1.1.182, 2.1.1.183 and 2.1.1.184 2.1.1.181, 2.1.1.182, 2.1.1.183 and 2.1.1.184] </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=2erc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2erc OCA], [https://pdbe.org/2erc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2erc RCSB], [https://www.ebi.ac.uk/pdbsum/2erc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2erc 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=2erc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2erc OCA], [https://pdbe.org/2erc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2erc RCSB], [https://www.ebi.ac.uk/pdbsum/2erc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2erc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/ERM_BACIU ERM_BACIU]] This protein produces a dimethylation of the adenine residue at position 2085 in 23S rRNA, resulting in reduced affinity between ribosomes and macrolide-lincosamide-streptogramin B antibiotics.<ref>PMID:12907737</ref> <ref>PMID:12946350</ref>		[https://www.uniprot.org/uniprot/ERM_BACIU ERM_BACIU] This protein produces a dimethylation of the adenine residue at position 2085 in 23S rRNA, resulting in reduced affinity between ribosomes and macrolide-lincosamide-streptogramin B antibiotics.<ref>PMID:12907737</ref> <ref>PMID:12946350</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2erc ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2erc ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	The prevalent mechanism of bacterial resistance to erythromycin and other antibiotics of the macrolide-lincosamide-streptogramin B group (MLS) is methylation of the 23S rRNA component of the 50S subunit in bacterial ribosomes. This sequence-specific methylation is catalyzed by the Erm group of methyltransferases (MTases). They are found in several strains of pathogenic bacteria, and ErmC is the most studied member of this class. The crystal structure of ErmC' (a naturally occurring variant of ErmC) from Bacillus subtilis has been determined at 3.0 A resolution by multiple anomalous diffraction phasing methods. The structure consists of a conserved alpha/beta amino-terminal domain which binds the cofactor S-adenosyl-l-methionine (SAM), followed by a smaller, alpha-helical RNA-recognition domain. The beta-sheet structure of the SAM-binding domain is well-conserved between the DNA, RNA, and small-molecule MTases. However, the C-terminal nucleic acid binding domain differs from the DNA-binding domains of other MTases and is unlike any previously reported RNA-recognition fold. A large, positively charged, concave surface is found at the interface of the N- and C-terminal domains and is proposed to form part of the protein-RNA interaction surface. ErmC' exhibits the conserved structural motifs previously found in the SAM-binding domain of other methyltransferases. A model of SAM bound to ErmC' is presented which is consistent with the motif conservation among MTases.

	Crystal structure of ErmC', an rRNA methyltransferase which mediates antibiotic resistance in bacteria.,Bussiere DE, Muchmore SW, Dealwis CG, Schluckebier G, Nienaber VL, Edalji RP, Walter KA, Ladror US, Holzman TF, Abad-Zapatero C Biochemistry. 1998 May 19;37(20):7103-12. PMID:9585521<ref>PMID:9585521</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 2erc" style="background-color:#fffaf0;"></div>~~
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Vibrio~~ subtilis ~~ehrenberg 1835~~]]		[[Category: Bacillus subtilis]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	~~[[Category: Transferase]]~~		[[Category: Abad-Zapatero C]]
	[[Category: Abad-Zapatero, C]]		[[Category: Bussiere DE]]
	[[Category: Bussiere~~, D E~~]]		[[Category: Dealwis CG]]
	[[Category: Dealwis~~, C G~~]]		[[Category: Muchmore SW]]
	[[Category: Muchmore~~, S W~~]]		[[Category: Schluckebier G]]
	[[Category: Schluckebier, G]]
	~~[[Category: Antibiotic resistance]]~~
	~~[[Category: Erythromycin resistance methylase css']]~~
	~~[[Category: Methyltransferase]]~~
	~~[[Category: Rrna methyltransferase~~]]

OCA at 12:26, 10 February 2021

2021-02-10T12:26:13Z

← Older revision		Revision as of 12:26, 10 February 2021
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	==CRYSTAL STRUCTURE OF ERMC' A RRNA-METHYL TRANSFERASE==		==CRYSTAL STRUCTURE OF ERMC' A RRNA-METHYL TRANSFERASE==
	<StructureSection load='2erc' size='340' side='right' caption='[[2erc]], [[Resolution\|resolution]] 3.03Å' scene=''>		<StructureSection load='2erc' size='340' side='right'caption='[[2erc]], [[Resolution\|resolution]] 3.03Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2erc]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ERC OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2ERC FirstGlance]. <br>		<table><tr><td colspan='2'>[[2erc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ERC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ERC FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ERMC' ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ERMC' ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Transferase Transferase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.181, 2.1.1.182, 2.1.1.183 and 2.1.1.184 2.1.1.181, 2.1.1.182, 2.1.1.183 and 2.1.1.184] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Transferase Transferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.181, 2.1.1.182, 2.1.1.183 and 2.1.1.184 2.1.1.181, 2.1.1.182, 2.1.1.183 and 2.1.1.184] </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=2erc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2erc OCA], [~~http~~://pdbe.org/2erc PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2erc RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2erc PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2erc 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=2erc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2erc OCA], [https://pdbe.org/2erc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2erc RCSB], [https://www.ebi.ac.uk/pdbsum/2erc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2erc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/ERM_BACIU ERM_BACIU]] This protein produces a dimethylation of the adenine residue at position 2085 in 23S rRNA, resulting in reduced affinity between ribosomes and macrolide-lincosamide-streptogramin B antibiotics.<ref>PMID:12907737</ref> <ref>PMID:12946350</ref>		[[https://www.uniprot.org/uniprot/ERM_BACIU ERM_BACIU]] This protein produces a dimethylation of the adenine residue at position 2085 in 23S rRNA, resulting in reduced affinity between ribosomes and macrolide-lincosamide-streptogramin B antibiotics.<ref>PMID:12907737</ref> <ref>PMID:12946350</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</StructureSection>		</StructureSection>
	[[Category: Vibrio subtilis ehrenberg 1835]]		[[Category: Vibrio subtilis ehrenberg 1835]]
			[[Category: Large Structures]]
	[[Category: Transferase]]		[[Category: Transferase]]
	[[Category: Abad-Zapatero, C]]		[[Category: Abad-Zapatero, C]]

OCA at 09:06, 14 June 2018

2018-06-14T09:06:43Z

← Older revision		Revision as of 09:06, 14 June 2018
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	==CRYSTAL STRUCTURE OF ERMC' A RRNA-METHYL TRANSFERASE==		==CRYSTAL STRUCTURE OF ERMC' A RRNA-METHYL TRANSFERASE==
	<StructureSection load='2erc' size='340' side='right' caption='[[2erc]], [[Resolution\|resolution]] 3.03Å' scene=''>		<StructureSection load='2erc' size='340' side='right' caption='[[2erc]], [[Resolution\|resolution]] 3.03Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2erc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"~~bacillus_globigii~~"~~_migula_1900~~ "~~bacillus globigii~~" ~~migula 1900~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ERC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ERC FirstGlance]. <br>		<table><tr><td colspan='2'>[[2erc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ERC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ERC FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ERMC' ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "~~Bacillus globigii~~" ~~Migula 1900~~])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ERMC' ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.181, 2.1.1.182, 2.1.1.183 and 2.1.1.184 2.1.1.181, 2.1.1.182, 2.1.1.183 and 2.1.1.184] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.181, 2.1.1.182, 2.1.1.183 and 2.1.1.184 2.1.1.181, 2.1.1.182, 2.1.1.183 and 2.1.1.184] </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=2erc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2erc OCA], [http://pdbe.org/2erc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2erc RCSB], [http://www.ebi.ac.uk/pdbsum/2erc 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=2erc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2erc OCA], [http://pdbe.org/2erc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2erc RCSB], [http://www.ebi.ac.uk/pdbsum/2erc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2erc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/er/2erc_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/er/2erc_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2erc ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Bacillus globigii migula 1900~~]]		[[Category: Vibrio subtilis ehrenberg 1835]]
	[[Category: Transferase]]		[[Category: Transferase]]
	[[Category: Abad-Zapatero, C]]		[[Category: Abad-Zapatero, C]]
Line 40:		Line 41:
	[[Category: Schluckebier, G]]		[[Category: Schluckebier, G]]
	[[Category: Antibiotic resistance]]		[[Category: Antibiotic resistance]]
	[[Category: Erythromycin resistance methylase cs']]		[[Category: Erythromycin resistance methylase css']]
	[[Category: Methyltransferase]]		[[Category: Methyltransferase]]
	[[Category: Rrna methyltransferase]]		[[Category: Rrna methyltransferase]]

OCA at 16:12, 11 September 2015

2015-09-11T16:12:29Z

← Older revision		Revision as of 16:12, 11 September 2015
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	<StructureSection load='2erc' size='340' side='right' caption='[[2erc]], [[Resolution\|resolution]] 3.03Å' scene=''>		<StructureSection load='2erc' size='340' side='right' caption='[[2erc]], [[Resolution\|resolution]] 3.03Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2erc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Bacillus_subtilis Bacillus subtilis~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ERC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ERC FirstGlance]. <br>		<table><tr><td colspan='2'>[[2erc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ERC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ERC FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ERMC' ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus ~~subtilis~~])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ERMC' ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/~~rRNA_(adenine-N(6)-)-methyltransferase rRNA (adenine-N(6)-)-methyltransferase~~], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.48 2.1.1.48] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.181, 2.1.1.182, 2.1.1.183 and 2.1.1.184 2.1.1.181, 2.1.1.182, 2.1.1.183 and 2.1.1.184] </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=2erc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2erc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2erc RCSB], [http://www.ebi.ac.uk/pdbsum/2erc 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=2erc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2erc OCA], [http://pdbe.org/2erc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2erc RCSB], [http://www.ebi.ac.uk/pdbsum/2erc PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/~~ERM_BACSU ERM_BACSU~~]] This protein produces a dimethylation of the adenine residue at position 2085 in 23S rRNA, resulting in reduced affinity between ribosomes and macrolide-lincosamide-streptogramin B antibiotics.<ref>PMID:~~12946350~~</ref> <ref>PMID:~~12907737~~</ref>		[[http://www.uniprot.org/uniprot/ERM_BACIU ERM_BACIU]] This protein produces a dimethylation of the adenine residue at position 2085 in 23S rRNA, resulting in reduced affinity between ribosomes and macrolide-lincosamide-streptogramin B antibiotics.<ref>PMID:12907737</ref> <ref>PMID:12946350</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 27:		Line 27:
	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 2erc" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Bacillus ~~subtilis~~]]		[[Category: Bacillus globigii migula 1900]]
			[[Category: Transferase]]
	[[Category: Abad-Zapatero, C]]		[[Category: Abad-Zapatero, C]]
	[[Category: Bussiere, D E]]		[[Category: Bussiere, D E]]

OCA at 18:51, 25 December 2014

2014-12-25T18:51:45Z

← Older revision		Revision as of 18:51, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2erc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ERC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ERC FirstGlance]. <br>		<table><tr><td colspan='2'>[[2erc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ERC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ERC FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ERMC' ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ERMC' ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])</td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/rRNA_(adenine-N(6)-)-methyltransferase rRNA (adenine-N(6)-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.48 2.1.1.48] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/rRNA_(adenine-N(6)-)-methyltransferase rRNA (adenine-N(6)-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.48 2.1.1.48] </span></td></tr>
	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2erc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2erc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2erc RCSB], [http://www.ebi.ac.uk/pdbsum/2erc 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=2erc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2erc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2erc RCSB], [http://www.ebi.ac.uk/pdbsum/2erc PDBsum]</span></td></tr>
	<table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/ERM_BACSU ERM_BACSU]] This protein produces a dimethylation of the adenine residue at position 2085 in 23S rRNA, resulting in reduced affinity between ribosomes and macrolide-lincosamide-streptogramin B antibiotics.<ref>PMID:12946350</ref> <ref>PMID:12907737</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</StructureSection>		</StructureSection>
	[[Category: Bacillus subtilis]]		[[Category: Bacillus subtilis]]
	[[Category: Abad-Zapatero, C.]]		[[Category: Abad-Zapatero, C]]
	[[Category: Bussiere, D E.]]		[[Category: Bussiere, D E]]
	[[Category: Dealwis, C G.]]		[[Category: Dealwis, C G]]
	[[Category: Muchmore, S W.]]		[[Category: Muchmore, S W]]
	[[Category: Schluckebier, G.]]		[[Category: Schluckebier, G]]
	[[Category: Antibiotic resistance]]		[[Category: Antibiotic resistance]]
	[[Category: Erythromycin resistance methylase cs']]		[[Category: Erythromycin resistance methylase cs']]
	[[Category: Methyltransferase]]		[[Category: Methyltransferase]]
	[[Category: Rrna methyltransferase]]		[[Category: Rrna methyltransferase]]

OCA at 02:49, 30 September 2014

2014-09-30T02:49:34Z

← Older revision		Revision as of 02:49, 30 September 2014
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	[[Image:~~2erc~~.~~png~~\|~~left~~\|~~200px~~]]		==CRYSTAL STRUCTURE OF ERMC' A RRNA-METHYL TRANSFERASE==
			<StructureSection load='2erc' size='340' side='right' caption='[[2erc]], [[Resolution\|resolution]] 3.03Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[2erc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ERC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ERC FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ERMC' ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])</td></tr>
			<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/rRNA_(adenine-N(6)-)-methyltransferase rRNA (adenine-N(6)-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.48 2.1.1.48] </span></td></tr>
			<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2erc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2erc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2erc RCSB], [http://www.ebi.ac.uk/pdbsum/2erc PDBsum]</span></td></tr>
			<table>
			== Evolutionary Conservation ==
			[[Image:Consurf_key_small.gif\|200px\|right]]
			Check<jmol>
			<jmolCheckbox>
			<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/er/2erc_consurf.spt"</scriptWhenChecked>
			<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
			<text>to colour the structure by Evolutionary Conservation</text>
			</jmolCheckbox>
			</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
			<div style="clear:both"></div>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			The prevalent mechanism of bacterial resistance to erythromycin and other antibiotics of the macrolide-lincosamide-streptogramin B group (MLS) is methylation of the 23S rRNA component of the 50S subunit in bacterial ribosomes. This sequence-specific methylation is catalyzed by the Erm group of methyltransferases (MTases). They are found in several strains of pathogenic bacteria, and ErmC is the most studied member of this class. The crystal structure of ErmC' (a naturally occurring variant of ErmC) from Bacillus subtilis has been determined at 3.0 A resolution by multiple anomalous diffraction phasing methods. The structure consists of a conserved alpha/beta amino-terminal domain which binds the cofactor S-adenosyl-l-methionine (SAM), followed by a smaller, alpha-helical RNA-recognition domain. The beta-sheet structure of the SAM-binding domain is well-conserved between the DNA, RNA, and small-molecule MTases. However, the C-terminal nucleic acid binding domain differs from the DNA-binding domains of other MTases and is unlike any previously reported RNA-recognition fold. A large, positively charged, concave surface is found at the interface of the N- and C-terminal domains and is proposed to form part of the protein-RNA interaction surface. ErmC' exhibits the conserved structural motifs previously found in the SAM-binding domain of other methyltransferases. A model of SAM bound to ErmC' is presented which is consistent with the motif conservation among MTases.

	~~{{STRUCTURE_2erc\| PDB=2erc \| SCENE= }}~~		Crystal structure of ErmC', an rRNA methyltransferase which mediates antibiotic resistance in bacteria.,Bussiere DE, Muchmore SW, Dealwis CG, Schluckebier G, Nienaber VL, Edalji RP, Walter KA, Ladror US, Holzman TF, Abad-Zapatero C Biochemistry. 1998 May 19;37(20):7103-12. PMID:9585521<ref>PMID:9585521</ref>

	~~===CRYSTAL STRUCTURE OF ERMC' A RRNA-METHYL TRANSFERASE===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_9585521}}~~		== References ==
			<references/>
	~~==About this Structure==~~		__TOC__
	~~[[2erc]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Bacillus_subtilis Bacillus subtilis]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2ERC OCA].~~		</StructureSection>

	==~~Reference~~==
	<~~ref group="xtra">PMID:009585521<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: Bacillus subtilis]]		[[Category: Bacillus subtilis]]
	[[Category: Abad-Zapatero, C.]]		[[Category: Abad-Zapatero, C.]]

OCA: Protected "2erc" [edit=sysop:move=sysop]

2013-01-06T12:00:32Z

Protected "2erc" [edit=sysop:move=sysop]

← Older revision	Revision as of 12:00, 6 January 2013
(No difference)

OCA at 12:00, 6 January 2013

2013-01-06T12:00:29Z

← Older revision		Revision as of 12:00, 6 January 2013
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	~~{{Seed}}~~
	[[Image:2erc.png\|left\|200px]]		[[Image:2erc.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_2erc", creates the "Structure Box" on the page.~~
	~~You may change the PDB parameter (which sets the PDB file loaded into the applet)~~
	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~
	~~or leave the SCENE parameter empty for the default display.~~
	~~-->~~
	{{STRUCTURE_2erc\| PDB=2erc \| SCENE= }}		{{STRUCTURE_2erc\| PDB=2erc \| SCENE= }}

	===CRYSTAL STRUCTURE OF ERMC' A RRNA-METHYL TRANSFERASE===		===CRYSTAL STRUCTURE OF ERMC' A RRNA-METHYL TRANSFERASE===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_9585521}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 9585521 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_9585521}}		{{ABSTRACT_PUBMED_9585521}}

	==About this Structure==		==About this Structure==
	~~2ERC~~ is a 2 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ERC OCA].		[[2erc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ERC OCA].

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~9585521~~</ref><references group="xtra"/>		<ref group="xtra">PMID:009585521</ref><references group="xtra"/>
	[[Category: Bacillus subtilis]]		[[Category: Bacillus subtilis]]
	[[Category: Abad-Zapatero, C.]]		[[Category: Abad-Zapatero, C.]]
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	[[Category: Methyltransferase]]		[[Category: Methyltransferase]]
	[[Category: Rrna methyltransferase]]		[[Category: Rrna methyltransferase]]

	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 03:11:07 2009''~~

OCA at 01:11, 18 February 2009

2009-02-18T01:11:11Z

← Older revision		Revision as of 01:11, 18 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
	2ERC is a ~~[[Single protein]]~~ structure of ~~sequence~~ from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ERC OCA].		2ERC is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ERC OCA].

	==Reference==		==Reference==
	Crystal structure of ErmC', an rRNA methyltransferase which mediates antibiotic resistance in bacteria., Bussiere DE, Muchmore SW, Dealwis CG, Schluckebier G, Nienaber VL, Edalji RP, Walter KA, Ladror US, Holzman TF, Abad-Zapatero C, Biochemistry. 1998 May 19;37(20):7103-12. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/9585521 9585521]~~		<ref group="xtra">PMID:9585521</ref><references group="xtra"/>
	[[Category: Bacillus subtilis]]		[[Category: Bacillus subtilis]]
	~~[[Category: Single protein]]~~
	[[Category: Abad-Zapatero, C.]]		[[Category: Abad-Zapatero, C.]]
	[[Category: Bussiere, D E.]]		[[Category: Bussiere, D E.]]
Line 36:		Line 35:
	[[Category: Rrna methyltransferase]]		[[Category: Rrna methyltransferase]]

	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Tue Jul 29 09~~:44:~~15 2008~~''		''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 03:11:07 2009''

OCA at 06:44, 29 July 2008

2008-07-29T06:44:21Z

← Older revision		Revision as of 06:44, 29 July 2008
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	[[Image:2erc.~~jpg~~\|left\|200px]]		{{Seed}}
			[[Image:2erc.png\|left\|200px]]

	<!--		<!--
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	{{STRUCTURE_2erc\| PDB=2erc \| SCENE= }}		{{STRUCTURE_2erc\| PDB=2erc \| SCENE= }}

	~~'''~~CRYSTAL STRUCTURE OF ERMC' A RRNA-METHYL TRANSFERASE~~'''~~		===CRYSTAL STRUCTURE OF ERMC' A RRNA-METHYL TRANSFERASE===


	~~==Overview==~~		<!--
	The ~~prevalent mechanism of bacterial resistance~~ to ~~erythromycin and other antibiotics of~~ the macrolide-lincosamide-streptogramin B group (MLS) is methylation of the 23S rRNA component of the 50S subunit in bacterial ribosomes. This sequence-specific methylation is catalyzed by the Erm group of methyltransferases (MTases). They are found in several strains of pathogenic bacteria, and ErmC is the most studied member of this class. The crystal structure of ErmC' (~~a naturally occurring variant of ErmC) from Bacillus subtilis has been determined~~ at 3.~~0 A resolution by multiple anomalous diffraction phasing methods~~. ~~The structure consists of a conserved alpha/beta amino-terminal domain which binds the cofactor S-adenosyl-l-methionine (SAM~~), ~~followed by a smaller, alpha-helical RNA-recognition domain. The beta-sheet structure of the SAM-binding domain~~ is ~~well-conserved between~~ the ~~DNA, RNA, and small-molecule MTases~~. ~~However, the C~~-~~terminal nucleic acid binding domain differs from the DNA~~-binding domains of other MTases and is unlike any previously reported RNA-recognition fold. A large, positively charged, concave surface is found at the interface of the N- and C-terminal domains and is proposed to form part of the protein-RNA interaction surface. ErmC' exhibits the conserved structural motifs previously found in the SAM-binding domain of other methyltransferases. A model of SAM bound to ErmC' is presented which is consistent with the motif conservation among MTases.		The line below this paragraph, {{ABSTRACT_PUBMED_9585521}}, adds the Publication Abstract to the page
			(as it appears on PubMed at http://www.pubmed.gov), where 9585521 is the PubMed ID number.
			-->
			{{ABSTRACT_PUBMED_9585521}}

	==About this Structure==		==About this Structure==
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	[[Category: Methyltransferase]]		[[Category: Methyltransferase]]
	[[Category: Rrna methyltransferase]]		[[Category: Rrna methyltransferase]]
	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 03~~:01:51 2008''
			''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:44:15 2008''