1YUB

SOLUTION STRUCTURE OF AN RRNA METHYLTRANSFERASE (ERMAM) THAT CONFERS MACROLIDE-LINCOSAMIDE-STREPTOGRAMIN ANTIBIOTIC RESISTANCE, NMR, MINIMIZED AVERAGE STRUCTURE

Summary for 1YUB

• Entry DOI: 10.2210/pdb1yub/pdb
• Descriptor: RRNA METHYLTRANSFERASE (1 entity in total)
• Functional Keywords: methyltransferase, erm, ermam, mls antibiotics, rrna
• Biological source: Streptococcus pneumoniae
• Total number of polymer chains: 1
• Total formula weight: 28862.57

Authors

Yu, L.,Petros, A.M.,Schnuchel, A.,Zhong, P.,Severin, J.M.,Walter, K.,Holzman, T.F.,Fesik, S.W. (deposition date: 1997-03-04, release date: 1998-03-04, Last modification date: 2024-05-22)

Primary citation

Yu, L.,Petros, A.M.,Schnuchel, A.,Zhong, P.,Severin, J.M.,Walter, K.,Holzman, T.F.,Fesik, S.W.
Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance.
Nat.Struct.Biol., 4:483-489, 1997

PubMed 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.

PubMed: 9187657
DOI: 10.1038/nsb0697-483

Experimental method

SOLUTION NMR