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

被引：85

作者：

Yu, LP ^{[1
]}

Petros, AM ^{[1
]}

Schnuchel, A ^{[1
]}

Zhong, P ^{[1
]}

Severin, JM ^{[1
]}

Walter, K ^{[1
]}

Holzman, TF ^{[1
]}

Fesik, SW ^{[1
]}

机构：

[1] ABBOTT LABS,DIV PHARMACEUT DISCOVERY,ABBOTT PK,IL 60064

来源：

NATURE STRUCTURAL BIOLOGY | 1997年 / 4卷 / 06期

关键词：

D O I：

10.1038/nsb0697-483

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 235 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.

引用

页码：483 / 489

页数：7

共 35 条

[1] Solution structure of the ribosomal RNA binding protein S15 from Thermus thermophilus [J].