Open AccessStructure of a putative trans ‐editing enzyme for prolyl‐tRNA synthetase from Aeropyrum pernix K1 at 1.7 Å resolution
Author(s) -
Murayama Kazutaka,
KatoMurayama Miyuki,
Katsura Kazushige,
UchikuboKamo Tomomi,
YamaguchiHirafuji Machiko,
Kawazoe Masahito,
Akasaka Ryogo,
HanawaSuetsugu Kyoko,
HoriTakemoto Chie,
Terada Takaho,
Shirouzu Mikako,
Yokoyama Shigeyuki
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309104032555
Subject(s) - monoclinic crystal system , caulobacter crescentus , crystal structure , crystallography , molecular replacement , agrobacterium tumefaciens , transfer rna , multiple isomorphous replacement , stereochemistry , haemophilus influenzae , biology , peptide sequence , chemistry , genetics , rna , gene , bacterial protein , bacteria , transgene
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 P 2 1 , 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% ( R free = 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‐tRNA Pro deacylase) from Haemophilus influenzae (HI1434; 22% sequence identity) and putative ProX proteins from Caulobacter crescentus (16%) and Agrobacterium tumefaciens (21%).