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Purification, crystallization and X‐ray crystallographic studies on a putative methyltransferase, YtqB, from Bacillus subtilis
Author(s) -
Park Sun Cheol,
Song Wan Seok,
Wi Jimin,
Yoon Sungil
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14004130
Subject(s) - bacillus subtilis , methyltransferase , escherichia coli , biochemistry , recombinant dna , methionine , bacteria , transferase , cofactor , biosynthesis , enzyme , chemistry , biology , methylation , function (biology) , gene , amino acid , microbiology and biotechnology , genetics
S ‐Adenosyl‐L‐methionine (SAM)‐dependent methyltransferases (MTases) catalyze the transfer of a methyl group from a SAM cofactor to specific substrate molecules, including small chemicals, proteins, DNAs and RNAs, and are required for various cellular functions, such as regulation of gene expression and biosynthesis of metabolites. Bacillus subtilis YtqB is a putative SAM‐dependent MTase whose biological function has not been characterized. To provide biochemical and structural insights into the role of YtqB in bacteria, the recombinant YtqB protein was overexpressed in the Escherichia coli expression system and purified by chromatographic methods. YtqB crystals were obtained in PEG‐containing conditions and diffracted to 1.68 Å resolution. The YtqB crystals belonged to space group P 2 1 2 1 2 1 , with two molecules in the asymmetric unit.