title: Crystallization and preliminary X-ray diffraction crystallographic study of tRNA m(1)A58 methyltransferase from Saccharomyces cerevisiae.
abstract: In Saccharomyces cerevisiae, TRM6 and TRM61 compose a tRNA methyltransferase which catalyzes the methylation of the N1 of adenine at position 58 in tRNAs, especially initiator methionine tRNA. TRM61 is the subunit that binds S-adenosyl-L-methionine and both subunits contribute to target tRNA binding. In order to elucidate the catalytic mechanism of TRM6-TRM61 and the mode of interaction between the two subunits, expression, purification, crystallization and X-ray diffraction analysis of the TRM6-TRM61 complex were performed in this study. The crystals diffracted to 2.80 Å resolution and belonged to the trigonal space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 139.14, c = 101.62 Å.
authors.affiliation: Hefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China.
authors.forename: Xiaoting
authors.initials: X
authors.lastname: Qiu
authors.forename: Kai
authors.initials: K
authors.lastname: Huang
authors.forename: Jinming
authors.initials: J
authors.lastname: Ma
authors.forename: Yongxiang
authors.initials: Y
authors.lastname: Gao
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D011485:Protein Binding; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism; D012359:tRNA Methyltransferases / Q000737:chemistry* / Q000378:metabolism
chemical_list: D029701:Saccharomyces cerevisiae Proteins; C409023:Gcd10 protein, S cerevisiae; D012359:tRNA Methyltransferases; C119384:GCD14 protein, S cerevisiae
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