The Escherichia coli YadB gene product reveals a novel aminoacyl-tRNA synthetase like activity
| Autor: | Christian Cambillau, Christophe Bignon, Daniel Y. Dubois, Renaud Vincentelli, Sacha Grisel, Silvia Spinelli, Jacques Lapointe, Valérie Campanacci, Daniel Kern, F. Pagot, Richard Giegé, Christel Valencia, Hubert Dominique Becker, Aurelia Salomoni |
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| Přispěvatelé: | Génétique moléculaire, génomique, microbiologie (GMGM), Université Louis Pasteur - Strasbourg I-Centre National de la Recherche Scientifique (CNRS), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS), Structure des macromolécules biologiques et mécanismes de reconnaissance (SMBMR), Centre National de la Recherche Scientifique (CNRS), Architecture et réactivité de l'ARN (ARN), Architecture et Réactivité de l'ARN (ARN), Institut de biologie moléculaire et cellulaire (IBMC), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA) |
| Rok vydání: | 2003 |
| Předmět: |
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Molecular Protein Conformation Molecular Sequence Data Glutamic Acid Biology Crystallography X-Ray Ligands Structural genomics Amino Acyl-tRNA Synthetases 03 medical and health sciences chemistry.chemical_compound Protein structure Adenosine Triphosphate Structural Biology Escherichia coli [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Molecular replacement Amino Acid Sequence tRNA Molecular Biology Peptide sequence 030304 developmental biology chemistry.chemical_classification 0303 health sciences Sequence Homology Amino Acid Aminoacyl tRNA synthetase Escherichia coli Proteins Thermus thermophilus 030302 biochemistry & molecular biology RNA Nuclear Proteins Adenosine Monophosphate RNA Transfer Glu Amino acid Neoplasm Proteins Glutamate-tRNA Ligase Kinetics Zinc Biochemistry chemistry Genes Bacterial Transfer RNA Carrier Proteins |
| Zdroj: | Journal of Molecular Biology Journal of Molecular Biology, Elsevier, 2004, 337 (2), pp.273-283. ⟨10.1016/j.jmb.2004.01.027⟩ |
| ISSN: | 0022-2836 1089-8638 |
| DOI: | 10.1016/j.jmb.2004.01.027⟩ |
| Popis: | 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 1.5Å 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. |
| Databáze: | OpenAIRE |
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