6brl

Crystal structure of a glutamate tRNA ligase from Elizabethkingia meningosepticum CCUG26117 in complex with its amino acid

spinqualitylabelsall models 6brl, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6brl is a 1 chain structure with sequence from Elizabethkingia meningoseptica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: EDO, GLU Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1T3HI54_ELIME Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).[HAMAP-Rule:MF_00022] Publication Abstract from PubMed 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 approximately 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. Crystal structures of glutamyl-tRNA synthetase from Elizabethkingia anopheles and E. meningosepticum.,Brooks L, Subramanian S, Dranow DM, Mayclin SJ, Myler PJ, Asojo OA Acta Crystallogr F Struct Biol Commun. 2022 Aug 1;78(Pt 8):306-312. doi: , 10.1107/S2053230X22007555. Epub 2022 Jul 28. PMID:35924598 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aminoacyl tRNA synthetase 3D structures

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