Publication Abstract from PubMed
S-adenosyl-l-methionine (SAM)-dependent methyltransferases (MTases) methylate diverse biological molecules using a SAM cofactor. The ytqB gene of Bacillus subtilis encodes a putative MTase and its biological function has never been characterized. To reveal the structural features and the cofactor binding mode of YtqB, we have determined the crystal structures of YtqB alone and in complex with its cofactor, SAM, at 1.9A and 2.2A resolutions, respectively. YtqB folds into a beta-sheet sandwiched by two alpha-helical layers, and assembles into a dimeric form. Each YtqB monomer contains one SAM binding site, which shapes SAM into a slightly curved conformation and exposes the reactive methyl group of SAM potentially to a substrate. Our comparative structural analysis of YtqB and its homologues indicates that YtqB is a SAM-dependent class I MTase, and provides insights into the substrate binding site of YtqB.
Structural analysis of a putative SAM-dependent methyltransferase, YtqB, from Bacillus subtilis.,Park SC, Song WS, Yoon SI Biochem Biophys Res Commun. 2014 Mar 14. pii: S0006-291X(14)00460-4. doi:, 10.1016/j.bbrc.2014.03.026. PMID:24637210[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
