title: Structure of a putative trans-editing enzyme for prolyl-tRNA synthetase from Aeropyrum pernix K1 at 1.7 A resolution.
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 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%).
authors.affiliation: RIKEN Genomic Sciences Center, Yokohama, Japan.
authors.forename: Kazutaka
authors.initials: K
authors.lastname: Murayama
authors.forename: Miyuki
authors.initials: M
authors.lastname: Kato-Murayama
authors.forename: Kazushige
authors.initials: K
authors.lastname: Katsura
authors.forename: Tomomi
authors.initials: T
authors.lastname: Uchikubo-Kamo
authors.forename: Machiko
authors.initials: M
authors.lastname: Yamaguchi-Hirafuji
authors.forename: Masahito
authors.initials: M
authors.lastname: Kawazoe
authors.forename: Ryogo
authors.initials: R
authors.lastname: Akasaka
authors.forename: Kyoko
authors.initials: K
authors.lastname: Hanawa-Suetsugu
authors.forename: Chie
authors.initials: C
authors.lastname: Hori-Takemoto
authors.forename: Takaho
authors.initials: T
authors.lastname: Terada
authors.forename: Mikako
authors.initials: M
authors.lastname: Shirouzu
authors.forename: Shigeyuki
authors.initials: S
authors.lastname: Yokoyama
mesh_terms: 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
chemical_list: D019843:Archaeal Proteins; D001426:Bacterial Proteins; D000604:Amino Acyl-tRNA Synthetases; C100134:prolyl T RNA synthetase