Crystallization and preliminary X-ray crystallographic studies of a mutant of ribosome recycling factor from Escherichia coli, Arg132Gly.
Ribosome recycling factor (RRF) plays a central role during the recycling of ribosomes in the final step of protein biosynthesis in prokaryotes and is therefore a favourable target for the development of new antibiotics. The crystal structure of Escherichia coli RRF has been reported to have an open L-shaped conformation, while other RRFs from thermophilic bacteria have a strict L-shaped conformation [Yun et al. (2000), Acta Cryst. D56, 84-85]. Wild-type E. coli RRF has so far not been crystallized free from bound detergent. Here, a mutant of RRF, Arg132Gly, has been crystallized without any detergent. A complete data set from a crystal of this mutant obtained by the hanging-drop vapour-diffusion method has been collected at 2.2 A resolution using synchrotron radiation at 100 K. The crystal belongs to the monoclinic space group P2(1), with unit-cell parameters a = 46.02, b = 49.27, c = 49.37 A, beta = 110.1 degrees. The currently refined structure indicates that RRF has a tRNA-like L-shaped conformation.
Nakano
Hiroaki
H
Graduate School of Pharmaceutical Sciences, Osaka University, 1-6 Yamadaoka, Suita, Osaka 565-0871, Japan.
Uchiyama
Susumu
S
Yoshida
Takuya
T
Ohkubo
Tadayasu
T
Kato
Hiroaki
H
Yamagata
Yuriko
Y
Kobayashi
Yuji
Y
D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry*; D009154:Mutation; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012269:Ribosomal Proteins
D011506:Proteins; D012269:Ribosomal Proteins; C087267:ribosome releasing factor