TY - JOUR
T1 - Crystallization and preliminary X-ray analysis of peptidyl-tRNA hydrolase from Escherichia coli in complex with the acceptor-TC domain of tRNA
AU - Ito, Kosuke
AU - Qi, Hao
AU - Shimizu, Yoshihiro
AU - Murakami, Ryo
AU - Miura, Kin Ichiro
AU - Ueda, Takuya
AU - Uchiumi, Toshio
PY - 2011/12
Y1 - 2011/12
N2 - 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-TC domain of tRNA using 1,4-butanediol as a precipitant. The crystals belonged to the hexagonal space group P61, 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-TC 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.
AB - 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-TC domain of tRNA using 1,4-butanediol as a precipitant. The crystals belonged to the hexagonal space group P61, 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-TC 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.
KW - acceptor-TC domain
KW - peptidyl-tRNA hydrolases
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U2 - 10.1107/S1744309111038383
DO - 10.1107/S1744309111038383
M3 - Article
C2 - 22139168
AN - SCOPUS:83055196772
VL - 67
SP - 1566
EP - 1569
JO - Acta Crystallographica Section F:Structural Biology Communications
JF - Acta Crystallographica Section F:Structural Biology Communications
SN - 1744-3091
IS - 12
ER -