1yub
From Proteopedia
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SOLUTION STRUCTURE OF AN RRNA METHYLTRANSFERASE (ERMAM) THAT CONFERS MACROLIDE-LINCOSAMIDE-STREPTOGRAMIN ANTIBIOTIC RESISTANCE, NMR, MINIMIZED AVERAGE STRUCTURE
Overview
The Erm family of methyltransferases is responsible for the development of, resistance to the macrolide-lincosamide-streptogramin type B (MLS), antibiotics. These enzymes methylate an adenine of 23S ribosomal RNA that, prevents the MLS antibiotics from binding to the ribosome and exhibiting, their antibacterial activity. Here we describe the three-dimensional, structure of an Erm family member, ErmAM, as determined by NMR, spectroscopy. The catalytic domain of ErmAM is structurally similar to, that found in other methyltransferases and consists of a seven-stranded, beta-sheet flanked by alpha-helices and a small two-stranded beta-sheet., In contrast to the catalytic domain, the substrate binding domain is, different from other methyltransferases and adopts a novel fold that, consists of four alpha-helices.
About this Structure
1YUB is a Single protein structure of sequence from Streptococcus pneumoniae. Active as rRNA (adenine-N(6)-)-methyltransferase, with EC number 2.1.1.48 Full crystallographic information is available from OCA.
Reference
Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance., Yu L, Petros AM, Schnuchel A, Zhong P, Severin JM, Walter K, Holzman TF, Fesik SW, Nat Struct Biol. 1997 Jun;4(6):483-9. PMID:9187657
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