Imagerie PI2

@article{,

title = {Sequence, overproduction and crystallization of aspartyl-tRNA synthetase from Thermus thermophilus. Implications for the structure of prokaryotic aspartyl-tRNA synthetases},

author = {A Poterszman and P Plateau and D Moras and S Blanquet and M H Mazauric and R Kreutzer and D Kern},

url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8319804},

isbn = {8319804},

year  = {1993},

date = {1993-01-01},

journal = {FEBS Lett},

volume = {325},

number = {3},

pages = {183-186},

abstract = {The genes of aspartyl-tRNA synthetase (AspRS) from two Thermus thermophilus strain VK-1 and HB8, have been cloned and sequenced. Their nucleotidic sequences code for the same protein which displays the three characteristic motifs of class II aminoacyl-tRNA synthetases. This enzyme shows 50% identity with Escherichia coli AspRS, over the totality of the chain (580 amino acids). A comparison with the eukaryotic yeast cytoplasmic AspRS indicates the presence in the prokaryotic AspRS of an extra domain between motifs 2 and 3 much larger than in the eukaryotic ones. When its gene is under the control of the tac promoter of the expression vector pKK223-3, the protein is efficiently overexpressed as a thermostable protein in E. coli. It can be further purified to homogeneity using a heat treatment followed by a single anion exchange chromatography. Single crystals of the pure protein, diffracting at least to 2.2 A resolution (space group P2(1)2(1)2(1)},

note = {0014-5793 

Journal Article},

keywords = {Amino Acid  Support, Amino Acid Sequence  Aspartate-tRNA Ligase/chemistry/*genetics/metabolism  Base Sequence  Cloning, Bacterial  Models, Molecular  Crystallization  Genes, Molecular  Molecular Sequence Data  Oligodeoxyribonucleotides  Sequence Homology, Non-U.S. Gov't  Thermus thermophilus/*enzymology/genetics, Unité ARN},

pubstate = {published},

tppubtype = {article}

}