6B1Z

Crystal Structure of Glutamate-tRNA Synthetase from Elizabethkingia anophelis

6B1Z の概要

• エントリーDOI: 10.2210/pdb6b1z/pdb
• 分子名称: Glutamate--tRNA ligase, FORMIC ACID, 1,2-ETHANEDIOL, ... (5 entities in total)
• 機能のキーワード: ssgcid, elizabethkingia anophelis, glutamate--trna ligase, ligase, structural genomics, seattle structural genomics center for infectious disease
• 由来する生物種: Elizabethkingia anophelis
• 細胞内の位置: Cytoplasm : A0A1T3FQP0
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 59832.06

構造登録者

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2017-09-19, 公開日: 2017-10-04, 最終更新日: 2024-07-03)

主引用文献

Brooks, L.,Subramanian, S.,Dranow, D.M.,Mayclin, S.J.,Myler, P.J.,Asojo, O.A.
Crystal structures of glutamyl-tRNA synthetase from Elizabethkingia anopheles and E. meningosepticum.
Acta Crystallogr.,Sect.F, 78:306-312, 2022

PubMed Abstract: Elizabethkingia bacteria are globally emerging pathogens that cause opportunistic and nosocomial infections, with up to 40% mortality among the immunocompromised. Elizabethkingia species are in the pipeline of organisms for high-throughput structural analysis at the Seattle Structural Genomics Center for Infectious Disease (SSGCID). These efforts include the structure-function analysis of potential therapeutic targets. Glutamyl-tRNA synthetase (GluRS) is essential for tRNA aminoacylation and is under investigation as a bacterial drug target. The SSGCID produced, crystallized and determined high-resolution structures of GluRS from E. meningosepticum (EmGluRS) and E. anopheles (EaGluRS). EmGluRS was co-crystallized with glutamate, while EaGluRS is an apo structure. EmGluRS shares ∼97% sequence identity with EaGluRS but less than 39% sequence identity with any other structure in the Protein Data Bank. EmGluRS and EaGluRS have the prototypical bacterial GluRS topology. EmGluRS and EaGluRS have similar binding sites and tertiary structures to other bacterial GluRSs that are promising drug targets. These structural similarities can be exploited for drug discovery.

PubMed: 35924598
DOI: 10.1107/S2053230X22007555

実験手法

X-RAY DIFFRACTION (1.6 Å)