Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 67, Issue -, Pages 1448-1450Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S174430911103733X
Keywords
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Funding
- USTC [KA207000007]
- Chinese National Natural Science Foundation [30025012, 10979039]
- Chinese Ministry of Science and Technology [2006CB806500, 2006CB910200, 2006AA02A318]
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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 angstrom 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 angstrom.
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