1qaq
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(New page: 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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Revision as of 22:25, 20 November 2007
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THE STRUCTURE OF THE RRNA METHYLTRANSFERASE ERMC': IMPLICATIONS FOR THE REACTION MECHANISM
Overview
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.
About this Structure
1QAQ is a Single protein structure of sequence from Bacillus subtilis with SFG as ligand. Active as rRNA (adenine-N(6)-)-methyltransferase, with EC number 2.1.1.48 Full crystallographic information is available from OCA.
Reference
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
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