PMID:22139168
| Citation |
Ito, K, Qi, H, Shimizu, Y, Murakami, R, Miura, K, Ueda, T and Uchiumi, T (2011) Crystallization and preliminary X-ray analysis of peptidyl-tRNA hydrolase from Escherichia coli in complex with the acceptor-TΨC domain of tRNA. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67:1566-9 |
|---|---|
| Abstract |
Peptidyl-tRNA hydrolase (Pth) cleaves the ester bond between the peptide and the tRNA of peptidyl-tRNA molecules, which are the product of aborted translation. In the present work, Pth from Escherichia coli was crystallized with the acceptor-TΨC domain of tRNA using 1,4-butanediol as a precipitant. The crystals belonged to the hexagonal space group P6(1), with unit-cell parameters a = b = 55.1, c = 413.1 Å, and diffracted X-rays beyond 2.4 Å resolution. The asymmetric unit is expected to contain two complexes of Pth and the acceptor-TΨC domain of tRNA (V(M) = 2.8 Å(3) Da(-1)), with a solvent content of 60.8%. The structure is being solved by molecular replacement. |
| Links |
PubMed PMC3232141 Online version:10.1107/S1744309111038383 |
| Keywords |
Carboxylic Ester Hydrolases/chemistry; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Models, Molecular; Protein Interaction Domains and Motifs; RNA, Transfer/chemistry; RNA, Transfer/metabolism |
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