Journal:Acta Cryst F:S2053230X22007555
From Proteopedia
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<scene name='91/917942/Cv/3'>EmGluRS monomer</scene> has a HUP-domain (orange), a Zn-binding-domain (green), and an anticodon binding domain (blue). The HUP domain and Zn-binding domain make up the N-terminal tRNA synthetases binding domain that binds the glutamate (spheres). | <scene name='91/917942/Cv/3'>EmGluRS monomer</scene> has a HUP-domain (orange), a Zn-binding-domain (green), and an anticodon binding domain (blue). The HUP domain and Zn-binding domain make up the N-terminal tRNA synthetases binding domain that binds the glutamate (spheres). | ||
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| + | <scene name='91/917942/Cv/4'>Superposed structures of EmGluRS (gray) and EaGluRS (cyan)</scene>. Mg2+ ion from EaGluRS is shown as a green sphere, glutamate molecule shown as spheres (colored by atoms with white, carbons, red, oxygen, and blue nitrogen spheres), formate and ethylene glycol from crystallization are shown as sticks (atoms colored in CPK). | ||
EmGluRS shares ~97% sequence identity with EaGluRS but less than 39% sequence identity with any other structures in the Protein Data Bank. EmGluRS and EaGluRS have prototypical bacterial GluRS topology. EmGluRS and EaGluRS have similar binding sites and tertiary structures to other bacterial GluRS that are promising drug targets. These structural similarities can be exploited for drug discovery. | EmGluRS shares ~97% sequence identity with EaGluRS but less than 39% sequence identity with any other structures in the Protein Data Bank. EmGluRS and EaGluRS have prototypical bacterial GluRS topology. EmGluRS and EaGluRS have similar binding sites and tertiary structures to other bacterial GluRS that are promising drug targets. These structural similarities can be exploited for drug discovery. | ||
Revision as of 13:48, 27 July 2022
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