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New page: left|200px<br /><applet load="2erc" size="450" color="white" frame="true" align="right" spinBox="true" caption="2erc, resolution 3.03Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:2erc.jpg|left|200px]]<br /><applet load="2erc" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2erc, resolution 3.03&Aring;" />
'''CRYSTAL STRUCTURE OF ERMC' A RRNA-METHYL TRANSFERASE'''<br />


==Overview==
==CRYSTAL STRUCTURE OF ERMC' A RRNA-METHYL TRANSFERASE==
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.
<StructureSection load='2erc' size='340' side='right'caption='[[2erc]], [[Resolution|resolution]] 3.03&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<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>
2ERC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ERC OCA].  
</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>
 
<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>
==Reference==
</table>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9585521 9585521]
== 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>
== 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/main_output.php?pdb_ID=2erc ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: rRNA (adenine-N(6)-)-methyltransferase]]
[[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 c']]
[[Category: methyltransferase]]
[[Category: rrna methyltransferase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:06:09 2007''

Latest revision as of 09:19, 14 February 2024

CRYSTAL STRUCTURE OF ERMC' A RRNA-METHYL TRANSFERASE

2erc, resolution 3.03Å

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