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Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance

Nature Structural Biology volume 4, pages 483–489 (1997)Cite this article

An Erratum to this article was published on 01 July 1997

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 β-sheet flanked by α-helices and a small two-stranded β-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 α-helices.

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Authors and Affiliations

  1. Pharmaceutical Discovery Division, Abbott Laboratories, Abbott Park, Illinois, 60064, USA

    Liping Yu, Andrew M. Petros, Arndt Schnuchel, Ping Zhong, Jean M. Severin, Karl Walter, Thomas F. Holzman & Stephen W. Fesik

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Correspondence to Stephen W. Fesik.

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Yu, L., Petros, A., Schnuchel, A. et al. Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance. Nat Struct Mol Biol 4, 483–489 (1997). https://doi.org/10.1038/nsb0697-483

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