1QAQ

THE STRUCTURE OF THE RRNA METHYLTRANSFERASE ERMC': IMPLICATIONS FOR THE REACTION MECHANISM

Summary for 1QAQ

• Entry DOI: 10.2210/pdb1qaq/pdb
• Descriptor: ERMC' RRNA METHYLTRANSFERASE, SINEFUNGIN (2 entities in total)
• Functional Keywords: binary complex with adenosyl-ornithine, transferase
• Biological source: Bacillus subtilis
• Total number of polymer chains: 1
• Total formula weight: 29336.92

Authors

Schluckebier, G.,Zhong, P.,Stewart, K.D.,Kavanaugh, T.J.,Abad-Zapatero, C. (deposition date: 1999-03-28, release date: 2000-03-29, Last modification date: 2024-02-14)

Primary citation

Schluckebier, G.,Zhong, P.,Stewart, K.D.,Kavanaugh, T.J.,Abad-Zapatero, C.
The 2.2 A structure of the rRNA methyltransferase ErmC' and its complexes with cofactor and cofactor analogs: implications for the reaction mechanism.
J.Mol.Biol., 289:277-291, 1999

PubMed Abstract: The rRNA methyltransferase ErmC' transfers methyl groups from S -adenosyl-l-methionine to atom N6 of an adenine base within the peptidyltransferase loop of 23 S rRNA, thus conferring antibiotic resistance against a number of macrolide antibiotics. The crystal structures of ErmC' and of its complexes with the cofactor S -adenosyl-l-methionine, the reaction product S-adenosyl-l-homocysteine and the methyltransferase inhibitor Sinefungin, respectively, show that the enzyme undergoes small conformational changes upon ligand binding. Overall, the ligand molecules bind to the protein in a similar mode as observed for other methyltransferases. Small differences between the binding of the amino acid parts of the different ligands are correlated with differences in their chemical structure. A model for the transition-state based on the atomic details of the active site is consistent with a one-step methyl-transfer mechanism and might serve as a first step towards the design of potent Erm inhibitors.

PubMed: 10366505
DOI: 10.1006/jmbi.1999.2788

Experimental method

X-RAY DIFFRACTION (2.8 Å)