| Literature DB >> 16508081 |
Kazutaka Murayama1, Miyuki Kato-Murayama, Kazushige Katsura, Tomomi Uchikubo-Kamo, Machiko Yamaguchi-Hirafuji, Masahito Kawazoe, Ryogo Akasaka, Kyoko Hanawa-Suetsugu, Chie Hori-Takemoto, Takaho Terada, Mikako Shirouzu, Shigeyuki 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 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%).Entities:
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Year: 2004 PMID： 16508081 PMCID： PMC1952386 DOI： 10.1107/S1744309104032555
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN： 1744-3091