1qao

<StructureSection load='1qao' size='340' side='right' caption='[[1qao]], [[Resolution|resolution]] 2.70&Aring;' scene=''>

<table><tr><td colspan='2'>[[1qao]] is a 1 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=1QAO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QAO FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></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=1qao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qao OCA], [http://pdbe.org/1qao PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qao RCSB], [http://www.ebi.ac.uk/pdbsum/1qao PDBsum]</span></td></tr>

[[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>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qa/1qao_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

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.

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:10366505<ref>PMID:10366505</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1qao" style="background-color:#fffaf0;"></div>

[[Category: Bacillus globigii migula 1900]]

[[Category: Transferase]]

[[Category: Abad-Zapatero, C]]

[[Category: Kavanaugh, T. J]]

[[Category: Schluckebier, G]]

[[Category: Stewart, K. D]]

[[Category: Zhong, P]]

[[Category: Binary complex with s-adenosylmethionine]]