1NZJ
Crystal Structure and Activity Studies of Escherichia Coli Yadb ORF
1NZJ の概要
| エントリーDOI | 10.2210/pdb1nzj/pdb |
| 分子名称 | Hypothetical protein yadB, ZINC ION (3 entities in total) |
| 機能のキーワード | zn cluster, glutamyl t-rna synthetase, structural genomics, unknown function |
| 由来する生物種 | Escherichia coli |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 33709.38 |
| 構造登録者 | Campanacci, V.,Kern, D.Y.,Becker, H.D.,Spinelli, S.,Valencia, C.,Vincentelli, R.,Pagot, F.,Bignon, C.,Giege, R.,Cambillau, C. (登録日: 2003-02-18, 公開日: 2004-04-13, 最終更新日: 2023-10-25) |
| 主引用文献 | 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. J.Mol.Biol., 337:273-283, 2004 Cited by PubMed 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. PubMed: 15003446DOI: 10.1016/j.jmb.2004.01.027 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.5 Å) |
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