TY - JOUR
T1 - Structure of a putative trans-editing enzyme for prolyl-tRNA synthetase from Aeropyrum pernix K1 at 1.7 Å resolution
AU - Murayama, Kazutaka
AU - Kato-Murayama, Miyuki
AU - Katsura, Kazushige
AU - Uchikubo-Kamo, Tomomi
AU - Yamaguchi-Hirafuji, MacHiko
AU - Kawazoe, Masahito
AU - Akasaka, Ryogo
AU - Hanawa-Suetsugu, Kyoko
AU - Hori-Takemoto, Chie
AU - Terada, Takaho
AU - Shirouzu, Mikako
AU - Yokoyama, Shigeyuki
PY - 2005
Y1 - 2005
N2 - The crystal structure of APE2540, the putative trans-editing enzyme ProX from Aeropyrum pernix K1, was determined in a high-throughput manner. The crystal belongs to the monoclinic space group P21, with unit-cell parameters a = 47.4, b = 58.9, c = 53.6 Å, β = 106.8°. The structure was solved by the multiwavelength anomalous dispersion method at 1.7 Å and refined to an R factor of 16.8% (Rfree = 20.5%). The crystal structure includes two protein molecules in the asymmetric unit. Each monomer consists of eight β-strands and seven α-helices. A structure-homology search revealed similarity between the trans-editing enzyme YbaK (or cysteinyl-tRNAPro deacylase) from Haemophilus influenzae (HI1434; 22% sequence identity) and putative ProX proteins from Caulobacter crescentus (16%) and Agrobacterium tumefaciens (21%).
AB - The crystal structure of APE2540, the putative trans-editing enzyme ProX from Aeropyrum pernix K1, was determined in a high-throughput manner. The crystal belongs to the monoclinic space group P21, with unit-cell parameters a = 47.4, b = 58.9, c = 53.6 Å, β = 106.8°. The structure was solved by the multiwavelength anomalous dispersion method at 1.7 Å and refined to an R factor of 16.8% (Rfree = 20.5%). The crystal structure includes two protein molecules in the asymmetric unit. Each monomer consists of eight β-strands and seven α-helices. A structure-homology search revealed similarity between the trans-editing enzyme YbaK (or cysteinyl-tRNAPro deacylase) from Haemophilus influenzae (HI1434; 22% sequence identity) and putative ProX proteins from Caulobacter crescentus (16%) and Agrobacterium tumefaciens (21%).
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U2 - 10.1107/S1744309104032555
DO - 10.1107/S1744309104032555
M3 - Article
C2 - 16508081
AN - SCOPUS:33646470984
SN - 1744-3091
VL - 61
SP - 26
EP - 29
JO - Acta Crystallographica Section F:Structural Biology Communications
JF - Acta Crystallographica Section F:Structural Biology Communications
IS - 1
ER -