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2erc

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[[Image:2erc.jpg|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF ERMC' A RRNA-METHYL TRANSFERASE==
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|PDB= 2erc |SIZE=350|CAPTION= <scene name='initialview01'>2erc</scene>, resolution 3.03&Aring;
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<StructureSection load='2erc' size='340' side='right'caption='[[2erc]], [[Resolution|resolution]] 3.03&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY= <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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.03&#8491;</td></tr>
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|GENE= ERMC' ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
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<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>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<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.ebi.ac.uk/pdbsum/2erc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2erc RCSB]</span>
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[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>
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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'''CRYSTAL STRUCTURE OF ERMC' A RRNA-METHYL TRANSFERASE'''
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/er/2erc_consurf.spt"</scriptWhenChecked>
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==Overview==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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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.
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==About this Structure==
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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].
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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].
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<div style="clear:both"></div>
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== References ==
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==Reference==
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<references/>
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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]
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__TOC__
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</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: rRNA (adenine-N(6)-)-methyltransferase]]
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[[Category: Abad-Zapatero C]]
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[[Category: Abad-Zapatero, C.]]
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[[Category: Bussiere DE]]
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[[Category: Bussiere, D E.]]
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[[Category: Dealwis CG]]
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[[Category: Dealwis, C G.]]
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[[Category: Muchmore SW]]
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[[Category: Muchmore, S W.]]
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[[Category: Schluckebier G]]
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[[Category: Schluckebier, G.]]
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[[Category: antibiotic resistance]]
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[[Category: erythromycin resistance methylase cs']]
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[[Category: methyltransferase]]
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[[Category: rrna methyltransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:52:46 2008''
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Current revision

CRYSTAL STRUCTURE OF ERMC' A RRNA-METHYL TRANSFERASE

PDB ID 2erc

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