6J7L

Crystal structure of Pseudomonas aeruginosa Earp in complex with TDP

Summary for 6J7L

• Entry DOI: 10.2210/pdb6j7l/pdb
• Descriptor: Pseudomonas aeruginosa Earp, THYMIDINE-5'-DIPHOSPHATE, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (4 entities in total)
• Functional Keywords: rhamnosyltransferase, transferase
• Biological source: Pseudomonas aeruginosa PAO1
• Total number of polymer chains: 1
• Total formula weight: 46728.59

Authors

He, C.,Li, F. (deposition date: 2019-01-18, release date: 2019-05-15, Last modification date: 2023-11-22)

Primary citation

He, 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

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

Experimental method

X-RAY DIFFRACTION (1.851 Å)