Crystal structure of a guanine nucleotide exchange factor encoded by the scrub typhus pathogen Orientia tsutsugamushi
Copyright policy )Crystal structure of a guanine nucleotide exchange factor encoded by the scrub typhus pathogen Orientia tsutsugamushi
Significance Scrub typhus is a neglected tropical disease caused by the bacterium Orientia tsutsugamushi . Although O. tsutsugamushi is an emerging public health threat, its pathogenic mechanisms remain markedly understudied. Bacterial pathogens subvert host actin dynamics by encoding guanine nucleotide exchange factors (GEFs) as effector proteins, which activate cellular Rho GTPases. Here, we identify a GEF domain within an O. tsutsugamushi protein that activates the host GTPase Rac1. While the overall shape of the GEF is similar to that of other bacterial effectors, the primary sequence, topology, and catalytic mechanism are completely distinct, suggesting convergent evolution. Our studies reveal a cryptic GEF domain encoded by O. tsutsugamushi and provide the groundwork to probe the role of cytoskeletal modulation in this neglected pathogen.
- Yale University United States
Models, Molecular, rac1 GTP-Binding Protein, rho GTP-Binding Proteins, Binding Sites, Protein Conformation, Crystallography, X-Ray, Orientia tsutsugamushi, Bacterial Proteins, Scrub Typhus, Multiprotein Complexes, Guanine Nucleotide Exchange Factors, Protein Interaction Domains and Motifs, Protein Binding
Models, Molecular, rac1 GTP-Binding Protein, rho GTP-Binding Proteins, Binding Sites, Protein Conformation, Crystallography, X-Ray, Orientia tsutsugamushi, Bacterial Proteins, Scrub Typhus, Multiprotein Complexes, Guanine Nucleotide Exchange Factors, Protein Interaction Domains and Motifs, Protein Binding
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