| Literature DB >> 9187657 |
L Yu1, A M Petros, A Schnuchel, P Zhong, J M Severin, K Walter, T F Holzman, S W Fesik.
Abstract
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.Entities:
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Year: 1997 PMID： 9187657 DOI： 10.1038/nsb0697-483
Source DB: PubMed Journal: Nat Struct Biol ISSN： 1072-8368