title: Crystallization and preliminary X-ray analysis of peptidyl-tRNA hydrolase from Escherichia coli in complex with the acceptor-TΨC domain of tRNA.
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.
authors.affiliation: Department of Biology, Faculty of Science, Niigata University, Nishi-ku, Niigata, Japan. k-ito@bio.sc.niigata-u.ac.jp
authors.forename: Kosuke
authors.initials: K
authors.lastname: Ito
authors.forename: Hao
authors.initials: H
authors.lastname: Qi
authors.forename: Yoshihiro
authors.initials: Y
authors.lastname: Shimizu
authors.forename: Ryo
authors.initials: R
authors.lastname: Murakami
authors.forename: Kin-ichiro
authors.initials: K
authors.lastname: Miura
authors.forename: Takuya
authors.initials: T
authors.lastname: Ueda
authors.forename: Toshio
authors.initials: T
authors.lastname: Uchiumi
mesh_terms: D002265:Carboxylic Ester Hydrolases / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D008958:Models, Molecular; D054730:Protein Interaction Domains and Motifs; D012343:RNA, Transfer / Q000737:chemistry* / Q000378:metabolism
chemical_list: D012343:RNA, Transfer; D002265:Carboxylic Ester Hydrolases; C019674:aminoacyl-tRNA hydrolase