3TZE

Crystal structure of a tryptophanyl-tRNA synthetase from Encephalitozoon cuniculi bound to tryptophan

3TZE の概要

• エントリーDOI: 10.2210/pdb3tze/pdb
• 関連するPDBエントリー: 2QUH 3FOC 3HV0 3HZR 3I05
• 分子名称: Tryptophanyl-tRNA synthetase, TRYPTOPHAN, POTASSIUM ION, ... (4 entities in total)
• 機能のキーワード: structural genomics, seattle structural genomics center for infectious disease, ssgcid, amino acylation, eukaryotic pathogen, microsporidia, fungi, intracellular parasite, ligase
• 由来する生物種: Encephalitozoon cuniculi (Microsporidian parasite)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 93628.90

構造登録者

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2011-09-27, 公開日: 2011-10-12, 最終更新日: 2023-09-13)

主引用文献

Moen, S.O.,Edwards, T.E.,Dranow, D.M.,Clifton, M.C.,Sankaran, B.,Van Voorhis, W.C.,Sharma, A.,Manoil, C.,Staker, B.L.,Myler, P.J.,Lorimer, D.D.
Ligand co-crystallization of aminoacyl-tRNA synthetases from infectious disease organisms.
Sci Rep, 7:223-223, 2017

PubMed Abstract: Aminoacyl-tRNA synthetases (aaRSs) charge tRNAs with their cognate amino acid, an essential precursor step to loading of charged tRNAs onto the ribosome and addition of the amino acid to the growing polypeptide chain during protein synthesis. Because of this important biological function, aminoacyl-tRNA synthetases have been the focus of anti-infective drug development efforts and two aaRS inhibitors have been approved as drugs. Several researchers in the scientific community requested aminoacyl-tRNA synthetases to be targeted in the Seattle Structural Genomics Center for Infectious Disease (SSGCID) structure determination pipeline. Here we investigate thirty-one aminoacyl-tRNA synthetases from infectious disease organisms by co-crystallization in the presence of their cognate amino acid, ATP, and/or inhibitors. Crystal structures were determined for a CysRS from Borrelia burgdorferi bound to AMP, GluRS from Borrelia burgdorferi and Burkholderia thailandensis bound to glutamic acid, a TrpRS from the eukaryotic pathogen Encephalitozoon cuniculi bound to tryptophan, a HisRS from Burkholderia thailandensis bound to histidine, and a LysRS from Burkholderia thailandensis bound to lysine. Thus, the presence of ligands may promote aaRS crystallization and structure determination. Comparison with homologous structures shows conformational flexibility that appears to be a recurring theme with this enzyme class.

PubMed: 28303005
DOI: 10.1038/s41598-017-00367-6

実験手法

X-RAY DIFFRACTION (2.6 Å)