1o9g

rRNA methyltransferase aviRa from Streptomyces viridochromogenes at 1.5A

spinqualitylabelsall models 1o9g, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1o9g is a 1 chain structure with sequence from "actinomyces_viridochromogenes"_krainsky_1914 "actinomyces viridochromogenes" krainsky 1914. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: MSE Related: 1qam, 1qan, 1qao, 1qaq, 1yub Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [AVRA_STRVR] Specifically methylates the guanine-2535 in 23S ribosomal RNA. Confers resistance to antibiotic avilamycin, an orthosomycin antibiotic. Publication Abstract from PubMed The emergence of antibiotic-resistant bacterial strains is a widespread problem in contemporary medical practice and drug design. It is therefore important to elucidate the underlying mechanism in each case. The methyltransferase AviRa from Streptomyces viridochromogenes mediates resistance to the antibiotic avilamycin, which is closely related to evernimicin, an oligosaccharide antibiotic that has been used in medical studies. The structure of AviRa was determined by X-ray diffraction at 1.5A resolution. Phases were obtained from one selenomethionine residue introduced by site-directed mutagenesis. The chain-fold is similar to that of most methyltransferases, although AviRa contains two additional helices as a specific feature. A putative-binding site for the cofactor S-adenosyl-L-methionine was derived from homologous structures. It agrees with the conserved pattern of interacting amino acid residues. AviRa methylates a specific guanine base within the peptidyltransferase loop of the 23S ribosomal RNA. Guided by the target, the enzyme was docked to the cognate ribosomal surface, where it fit well into a deep cleft without contacting any ribosomal protein. The two additional alpha-helices of AviRa filled a depression in the surface. Since the transferred methyl group of the cofactor is in a pocket beneath the enzyme surface, the targeted guanine base has to flip out for methylation. Crystal structure of the avilamycin resistance-conferring methyltransferase AviRa from Streptomyces viridochromogenes.,Mosbacher TG, Bechthold A, Schulz GE J Mol Biol. 2003 May 23;329(1):147-57. PMID:12742024 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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