2erc
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(New page: 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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Revision as of 07:58, 21 November 2007
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CRYSTAL STRUCTURE OF ERMC' A RRNA-METHYL TRANSFERASE
Overview
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.
About this Structure
2ERC is a Single protein structure of sequence from Bacillus subtilis. Active as rRNA (adenine-N(6)-)-methyltransferase, with EC number 2.1.1.48 Full crystallographic information is available from OCA.
Reference
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:9585521
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