ArticleActa crystallographica. Section F, Structural biology communications2022
Crystal structures of glutamyl-tRNA synthetase from Elizabethkingia anopheles and E. meningosepticum.
Article in Acta crystallographica. Section F, Structural biology communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Using resources generated by the Seattle Structural Genomics Center for Infectious Disease (SSGCID) for training early career researchers.Acta crystallographica. Section F, Structural biology communications · 2025Article
- Architecture ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Crystal structure of glutamyl-tRNA synthetase from Helicobacter pylori.Acta crystallographica. Section F, Structural biology communications · 2024Article
- Structures of Brucella ovis leucine-, isoleucine-, valine-, threonine- and alanine-binding protein reveal a conformationally flexible peptide-binding cavity.Acta crystallographica. Section F, Structural biology communications · 2024Article
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Authors and funding
6 authors.
Funding
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.
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