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
; 61(Pt 1): 26-9, 2005 Jan 01.
Article
in En
| MEDLINE
| ID: mdl-16508081
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%).
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Aeropyrum
/
Amino Acyl-tRNA Synthetases
Type of study:
Prognostic_studies
Language:
En
Journal:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Year:
2005
Document type:
Article
Affiliation country:
Japan