期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 446, 期 4, 页码 921-926出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2014.03.026
关键词
Bacillus subtilis; YtqB; Methyltransferase; S-adenosyl-L-methionine; Crystal structure
资金
- Basic Science Research Program through National Research Foundation of Korea (NRF) - Ministry of Science, ICT Future Planning [2012R1A1A1003701]
- Research Grant from Kangwon National University
- National Research Foundation of Korea [2012R1A1A1003701] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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 1.9 angstrom and 2.2 angstrom resolutions, respectively. YtqB folds into a beta-sheet sandwiched by two a-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. (C) 2014 Elsevier Inc. All rights reserved.
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