Your browser version may not work well with NCBI's Web applications. More information here...
1: Nat Struct Biol. 1997 Jun;4(6):483-9.Links
Erratum in:
Nat Struct Biol 1997 Jul;4(7):592.
Comment in:
Nat Struct Biol. 1997 Jun;4(6):421-2.

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.

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

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.

PMID: 9187657 [PubMed - indexed for MEDLINE]