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6J7L

Crystal structure of Pseudomonas aeruginosa Earp in complex with TDP

Summary for 6J7L
Entry DOI10.2210/pdb6j7l/pdb
DescriptorPseudomonas aeruginosa Earp, THYMIDINE-5'-DIPHOSPHATE, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (4 entities in total)
Functional Keywordsrhamnosyltransferase, transferase
Biological sourcePseudomonas aeruginosa PAO1
Total number of polymer chains1
Total formula weight46728.59
Authors
He, C.,Li, F. (deposition date: 2019-01-18, release date: 2019-05-15, Last modification date: 2023-11-22)
Primary citationHe, C.,Liu, N.,Li, F.,Jia, X.,Peng, H.,Liu, Y.,Xiao, Y.
Complex Structure ofPseudomonas aeruginosaArginine Rhamnosyltransferase EarP with Its Acceptor Elongation Factor P.
J.Bacteriol., 201:-, 2019
Cited by
PubMed Abstract: A bacterial inverting glycosyltransferase EarP transfers rhamnose from dTDP-β-l-rhamnose (TDP-Rha) to Arg32 of translation elongation factor P (EF-P) to activate its function. We report here the structural and biochemical characterization of EarP. In contrast to recently reported EarP, EarP exhibits differential conformational changes upon TDP-Rha and EF-P binding. Sugar donor binding enhances acceptor binding to EarP, as revealed by structural comparison between the apo-, TDP-Rha-, and TDP/EF-P-bound forms and isothermal titration calorimetry experiments. EF-P rhamnosylation combined with active-site geometry indicates that Asp16 corresponding to Asp20 of EarP is the catalytic base, whereas Glu272 is another putative catalytic residue. Our study should provide the basis for EarP-targeted inhibitor design against infections from and other clinically relevant species. Posttranslational rhamnosylation of EF-P plays a key role in , establishing virulence and antibiotic resistance, as well as survival. The detailed structural and biochemical characterization of the EF-P-specific rhamnosyltransferase EarP from not only demonstrates that sugar donor TDP-Rha binding enhances acceptor EF-P binding to EarP but also should provide valuable information for the structure-guided development of its inhibitors against infections from and other EarP-containing pathogens.
PubMed: 31010899
DOI: 10.1128/JB.00128-19
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.851 Å)
Structure validation

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