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New page: left|200px<br /><applet load="1qaq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qaq, resolution 2.8Å" /> '''THE STRUCTURE OF THE ...
 
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[[Image:1qaq.jpg|left|200px]]<br /><applet load="1qaq" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1qaq, resolution 2.8&Aring;" />
'''THE STRUCTURE OF THE RRNA METHYLTRANSFERASE ERMC': IMPLICATIONS FOR THE REACTION MECHANISM'''<br />


==Overview==
==THE STRUCTURE OF THE RRNA METHYLTRANSFERASE ERMC': IMPLICATIONS FOR THE REACTION MECHANISM==
The rRNA methyltransferase ErmC' transfers methyl groups from S, -adenosyl-l-methionine to atom N6 of an adenine base within the, peptidyltransferase loop of 23 S rRNA, thus conferring antibiotic, resistance against a number of macrolide antibiotics. The crystal, structures of ErmC' and of its complexes with the cofactor S, -adenosyl-l-methionine, the reaction product S-adenosyl-l-homocysteine and, the methyltransferase inhibitor Sinefungin, respectively, show that the, enzyme undergoes small conformational changes upon ligand binding., Overall, the ligand molecules bind to the protein in a similar mode as, observed for other methyltransferases. Small differences between the, binding of the amino acid parts of the different ligands are correlated, with differences in their chemical structure. A model for the, transition-state based on the atomic details of the active site is, consistent with a one-step methyl-transfer mechanism and might serve as a, first step towards the design of potent Erm inhibitors.
<StructureSection load='1qaq' size='340' side='right'caption='[[1qaq]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1qaq]] is a 1 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=1QAQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QAQ FirstGlance]. <br>
1QAQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with SFG as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1QAQ 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]] 2.8&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SFG:SINEFUNGIN'>SFG</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qaq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qaq OCA], [https://pdbe.org/1qaq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qaq RCSB], [https://www.ebi.ac.uk/pdbsum/1qaq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qaq ProSAT]</span></td></tr>
The 2.2 A structure of the rRNA methyltransferase ErmC' and its complexes with cofactor and cofactor analogs: implications for the reaction mechanism., Schluckebier G, Zhong P, Stewart KD, Kavanaugh TJ, Abad-Zapatero C, J Mol Biol. 1999 Jun 4;289(2):277-91. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10366505 10366505]
</table>
== 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/qa/1qaq_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=1qaq 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: Kavanaugh TJ]]
[[Category: Kavanaugh, T. J.]]
[[Category: Schluckebier G]]
[[Category: Schluckebier, G.]]
[[Category: Stewart KD]]
[[Category: Stewart, K. D.]]
[[Category: Zhong P]]
[[Category: Zhong, P.]]
[[Category: SFG]]
[[Category: binary complex with adenosyl-ornithine]]
 
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