Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 61, Part 1 (January 2005)

structural genomics communications

Acta Cryst. (2005). F61, 26-29 [ doi:10.1107/S1744309104032555 ]

Structure of a putative trans-editing enzyme for prolyl-tRNA synthetase from Aeropyrum pernix K1 at 1.7 Å resolution

K. Murayama, M. Kato-Murayama, K. Katsura, T. Uchikubo-Kamo, M. Yamaguchi-Hirafuji, M. Kawazoe, R. Akasaka, K. Hanawa-Suetsugu, C. Hori-Takemoto, T. Terada, M. Shirouzu and S. Yokoyama

Abstract: 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, [beta] = 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% (R_free = 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-tRNA^Pro deacylase) from Haemophilus influenzae (HI1434; 22% sequence identity) and putative ProX proteins from Caulobacter crescentus (16%) and Agrobacterium tumefaciens (21%).

PDB reference: 1wdv

Keywords: trans-editing enzymes; APE2540.