1yub

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(New page: 200px<br /><applet load="1yub" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yub" /> '''SOLUTION STRUCTURE OF AN RRNA METHYLTRANSFER...)
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[[Image:1yub.jpg|left|200px]]<br /><applet load="1yub" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1yub" />
 
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'''SOLUTION STRUCTURE OF AN RRNA METHYLTRANSFERASE (ERMAM) THAT CONFERS MACROLIDE-LINCOSAMIDE-STREPTOGRAMIN ANTIBIOTIC RESISTANCE, NMR, MINIMIZED AVERAGE STRUCTURE'''<br />
 
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==Overview==
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==SOLUTION STRUCTURE OF AN RRNA METHYLTRANSFERASE (ERMAM) THAT CONFERS MACROLIDE-LINCOSAMIDE-STREPTOGRAMIN ANTIBIOTIC RESISTANCE, NMR, MINIMIZED AVERAGE STRUCTURE==
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The Erm family of methyltransferases is responsible for the development of, resistance to the macrolide-lincosamide-streptogramin type B (MLS), antibiotics. These enzymes methylate an adenine of 23S ribosomal RNA that, prevents the MLS antibiotics from binding to the ribosome and exhibiting, their antibacterial activity. Here we describe the three-dimensional, structure of an Erm family member, ErmAM, as determined by NMR, spectroscopy. The catalytic domain of ErmAM is structurally similar to, that found in other methyltransferases and consists of a seven-stranded, beta-sheet flanked by alpha-helices and a small two-stranded beta-sheet., In contrast to the catalytic domain, the substrate binding domain is, different from other methyltransferases and adopts a novel fold that, consists of four alpha-helices.
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<StructureSection load='1yub' size='340' side='right'caption='[[1yub]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1yub]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YUB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YUB FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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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=1yub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yub OCA], [https://pdbe.org/1yub PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yub RCSB], [https://www.ebi.ac.uk/pdbsum/1yub PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yub ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ERM_STREE ERM_STREE] 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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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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/yu/1yub_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1yub ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The Erm family of methyltransferases is responsible for the development of resistance to the macrolide-lincosamide-streptogramin type B (MLS) antibiotics. These enzymes methylate an adenine of 23S ribosomal RNA that prevents the MLS antibiotics from binding to the ribosome and exhibiting their antibacterial activity. Here we describe the three-dimensional structure of an Erm family member, ErmAM, as determined by NMR spectroscopy. The catalytic domain of ErmAM is structurally similar to that found in other methyltransferases and consists of a seven-stranded beta-sheet flanked by alpha-helices and a small two-stranded beta-sheet. In contrast to the catalytic domain, the substrate binding domain is different from other methyltransferases and adopts a novel fold that consists of four alpha-helices.
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==About this Structure==
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Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance.,Yu L, Petros AM, Schnuchel A, Zhong P, Severin JM, Walter K, Holzman TF, Fesik SW Nat Struct Biol. 1997 Jun;4(6):483-9. PMID:9187657<ref>PMID:9187657</ref>
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1YUB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. 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=1YUB OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance., Yu L, Petros AM, Schnuchel A, Zhong P, Severin JM, Walter K, Holzman TF, Fesik SW, Nat Struct Biol. 1997 Jun;4(6):483-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9187657 9187657]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 1yub" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Streptococcus pneumoniae]]
[[Category: Streptococcus pneumoniae]]
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[[Category: rRNA (adenine-N(6)-)-methyltransferase]]
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[[Category: Fesik SW]]
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[[Category: Fesik, S.W.]]
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[[Category: Holzman TF]]
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[[Category: Holzman, T.F.]]
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[[Category: Petros AM]]
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[[Category: Petros, A.M.]]
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[[Category: Schnuchel A]]
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[[Category: Schnuchel, A.]]
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[[Category: Severin JM]]
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[[Category: Severin, J.M.]]
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[[Category: Walter K]]
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[[Category: Walter, K.]]
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[[Category: Yu L]]
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[[Category: Yu, L.]]
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[[Category: Zhong P]]
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[[Category: Zhong, P.]]
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[[Category: erm]]
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[[Category: ermam]]
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[[Category: methyltransferase]]
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[[Category: mls antibiotics]]
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[[Category: nmr]]
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[[Category: rrna]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:03:24 2007''
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Current revision

SOLUTION STRUCTURE OF AN RRNA METHYLTRANSFERASE (ERMAM) THAT CONFERS MACROLIDE-LINCOSAMIDE-STREPTOGRAMIN ANTIBIOTIC RESISTANCE, NMR, MINIMIZED AVERAGE STRUCTURE

PDB ID 1yub

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