Journal article
Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance
Nature structural biology, Vol.4(6), pp.483-489
06/1997
DOI: 10.1038/nsb0697-483
PMID: 9187657
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.
Details
- Title: Subtitle
- Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance
- Creators
- Liping Yu - Discovery LaboratoriesAndrew M. Petros - Discovery LaboratoriesArndt Schnuchel - Discovery LaboratoriesPing Zhong - Discovery LaboratoriesJean M. Severin - Discovery LaboratoriesKarl Walter - Discovery LaboratoriesThomas F. Holzman - AbbottStephen W. Fesik - Discovery Laboratories
- Resource Type
- Journal article
- Publication Details
- Nature structural biology, Vol.4(6), pp.483-489
- DOI
- 10.1038/nsb0697-483
- PMID
- 9187657
- ISSN
- 1072-8368
- eISSN
- 2331-365X
- Language
- English
- Date published
- 06/1997
- Academic Unit
- Biochemistry and Molecular Biology; Medicine Administration
- Record Identifier
- 9984627242102771
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