Journal:Acta Cryst F:S2053230X24011099

spinqualitylabelsall models Overall structure of HpGluRS monomer 6b1p in rainbow color from blue N-terminus to red C-terminus. Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Crystal structure of glutamyl-tRNA synthetase from Helicobacter pylori Dr Oluwatoyin A. Asojo Molecular Tour Helicobacter pylori is one of the most common bacterial infections; over two-thirds of the world’s population is infected by early childhood. Persistent H. pylori infection results in gastric ulcers and cancers. Due to drug resistance, there is a need to develop alternative treatments to clear H. pylori. The Seattle Structural Genomics Center for Infectious Disease (SSGCID) conducts structure-function analysis of potential therapeutic targets from H. pylori. Glutamyl-tRNA synthetase (GluRS) is essential for tRNA aminoacylation and is under investigation as a bacterial drug target. The SSGCID produced, crystallized, and determined the apo structure of H. pylori GluRS (HpGluRS). HpGluRS has the prototypical bacterial GluRS topology, similar binding sites, and tertiary structures with other bacterial GluRS that are promising drug targets. ENDScript analysis reveals that HpGluRS is a prototypical bacterial GluRS shown showing sequence conservation as a ribbon diagram and solvent-accessible surface area Residues involved in glutamate binding are well conserved with Pseudomonas aeruginosa GluRS (PaGluRS), which has been studied to develop promising new inhibitors for Pseudomonas aeruginosa. These structural similarities can be exploited for drug discovery and repurposing to generate new antibacterials to clear persistent H. pylori infection and reduce gastric ulcers and cancer. References

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