Campanacci V, Dubois D Y, Becker H D, Kern D, Spinelli S, Valencia C, Pagot F, Salomoni A, Grisel S, Vincentelli R, Bignon C, Lapointe J, Giege R, Cambillau C
The Escherichia coli YadB gene product reveals a novel aminoacyl-tRNA synthetase like activity Article de journal
Dans: J Mol Biol, vol. 337, no. 2, p. 273-283, 2004, ISBN: 15003446, (0022-2836 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Amino Acid Support, Bacterial Glutamate-tRNA Ligase/chemistry/genetics/metabolism Glutamic Acid/metabolism Kinetics Ligands Models, Glu/metabolism Sequence Homology, KERN GIEGE Adenosine Monophosphate/metabolism Adenosine Triphosphate/metabolism Amino Acid Sequence Amino Acyl-tRNA Ligases/chemistry/*genetics/*metabolism Carrier Proteins/metabolism Crystallography, Molecular Molecular Sequence Data Neoplasm Proteins/metabolism Nuclear Proteins/metabolism Protein Conformation RNA, Non-U.S. Gov't Thermus thermophilus/enzymology/genetics Zinc/metabolism, Transfer, Unité ARN, X-Ray Escherichia coli/*enzymology/*genetics Escherichia coli Proteins/chemistry/*genetics/*metabolism Genes
@article{,
title = {The Escherichia coli YadB gene product reveals a novel aminoacyl-tRNA synthetase like activity},
author = {V Campanacci and D Y Dubois and H D Becker and D Kern and S Spinelli and C Valencia and F Pagot and A Salomoni and S Grisel and R Vincentelli and C Bignon and J Lapointe and R Giege and C Cambillau},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15003446},
isbn = {15003446},
year = {2004},
date = {2004-01-01},
journal = {J Mol Biol},
volume = {337},
number = {2},
pages = {273-283},
abstract = {In the course of a structural genomics program aiming at solving the structures of Escherichia coli open reading frame products of unknown function, we have determined the structure of YadB at 1.5A using molecular replacement. The YadB protein is 298 amino acid residues long and displays 34% sequence identity with E.coli glutamyl-tRNA synthetase (GluRS). It is much shorter than GluRS, which contains 468 residues, and lacks the complete domain interacting with the tRNA anticodon loop. As E.coli GluRS, YadB possesses a Zn2+ located in the putative tRNA acceptor stem-binding domain. The YadB cluster uses cysteine residues as the first three zinc ligands, but has a weaker tyrosine ligand at the fourth position. It shares with canonical amino acid RNA synthetases a major functional feature, namely activation of the amino acid (here glutamate). It differs, however, from GluRSs by the fact that the activation step is tRNA-independent and that it does not catalyze attachment of the activated glutamate to E.coli tRNAGlu, but to another, as yet unknown tRNA. These results suggest thus a novel function, distinct from that of GluRSs, for the yadB gene family.},
note = {0022-2836
Journal Article},
keywords = {Amino Acid Support, Bacterial Glutamate-tRNA Ligase/chemistry/genetics/metabolism Glutamic Acid/metabolism Kinetics Ligands Models, Glu/metabolism Sequence Homology, KERN GIEGE Adenosine Monophosphate/metabolism Adenosine Triphosphate/metabolism Amino Acid Sequence Amino Acyl-tRNA Ligases/chemistry/*genetics/*metabolism Carrier Proteins/metabolism Crystallography, Molecular Molecular Sequence Data Neoplasm Proteins/metabolism Nuclear Proteins/metabolism Protein Conformation RNA, Non-U.S. Gov't Thermus thermophilus/enzymology/genetics Zinc/metabolism, Transfer, Unité ARN, X-Ray Escherichia coli/*enzymology/*genetics Escherichia coli Proteins/chemistry/*genetics/*metabolism Genes},
pubstate = {published},
tppubtype = {article}
}