Structure of a putative trans-editing enzyme for prolyl-tRNA synthetase from Aeropyrum pernix K1 at 1.7 A resolution.
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 P2(1), with unit-cell parameters a = 47.4, b = 58.9, c = 53.6 A, beta = 106.8 degrees. The structure was solved by the multiwavelength anomalous dispersion method at 1.7 A 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 beta-strands and seven alpha-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%).
Murayama
Kazutaka
K
RIKEN Genomic Sciences Center, Yokohama, Japan.
Kato-Murayama
Miyuki
M
Katsura
Kazushige
K
Uchikubo-Kamo
Tomomi
T
Yamaguchi-Hirafuji
Machiko
M
Kawazoe
Masahito
M
Akasaka
Ryogo
R
Hanawa-Suetsugu
Kyoko
K
Hori-Takemoto
Chie
C
Terada
Takaho
T
Shirouzu
Mikako
M
Yokoyama
Shigeyuki
S
D041522:Aeropyrum / Q000201:enzymology*; D000595:Amino Acid Sequence; D000604:Amino Acyl-tRNA Synthetases / Q000737:chemistry* / Q000378:metabolism; D019843:Archaeal Proteins / Q000737:chemistry / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D006193:Haemophilus influenzae / Q000201:enzymology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid
D019843:Archaeal Proteins; D001426:Bacterial Proteins; D000604:Amino Acyl-tRNA Synthetases; C100134:prolyl T RNA synthetase