Structural highlights
Function
Q9Y8U3_AERPE
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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%).
Structure of a putative trans-editing enzyme for prolyl-tRNA synthetase from Aeropyrum pernix K1 at 1.7 A resolution.,Murayama K, Kato-Murayama M, Katsura K, Uchikubo-Kamo T, Yamaguchi-Hirafuji M, Kawazoe M, Akasaka R, Hanawa-Suetsugu K, Hori-Takemoto C, Terada T, Shirouzu M, Yokoyama S Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jan 1;61(Pt, 1):26-9. Epub 2004 Dec 24. PMID:16508081[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Murayama K, Kato-Murayama M, Katsura K, Uchikubo-Kamo T, Yamaguchi-Hirafuji M, Kawazoe M, Akasaka R, Hanawa-Suetsugu K, Hori-Takemoto C, Terada T, Shirouzu M, Yokoyama S. Structure of a putative trans-editing enzyme for prolyl-tRNA synthetase from Aeropyrum pernix K1 at 1.7 A resolution. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jan 1;61(Pt, 1):26-9. Epub 2004 Dec 24. PMID:16508081 doi:10.1107/S1744309104032555
