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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.

SUBMITTER: Qiu X

PROVIDER: S-EPMC3212473 | biostudies-literature | 2011 Nov

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction crystallographic study of tRNA m(1)A58 methyltransferase from Saccharomyces cerevisiae.

Qiu Xiaoting X Huang Kai K Ma Jinming J Gao Yongxiang Y

Acta crystallographica. Section F, Structural biology and crystallization communications 20111027 Pt 11

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 ...[more]

PMID: 22102254

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