5CPC

Crystal structure of SopD, a type III secreted virulence effector from Salmonella enterica

Summary for 5CPC

• Entry DOI: 10.2210/pdb5cpc/pdb
• Related: 5CQ9
• Descriptor: Secreted effector protein SopD (2 entities in total)
• Functional Keywords: t3ss effector protein, structural genomics, montreal-kingston bacterial structural genomics initiative, bsgi, cell invasion
• Biological source: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
• Total number of polymer chains: 2
• Total formula weight: 72376.45

Authors

Shi, R.,Cygler, M.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (deposition date: 2015-07-21, release date: 2015-09-09, Last modification date: 2024-03-06)

Primary citation

D'Costa, V.M.,Braun, V.,Landekic, M.,Shi, R.,Proteau, A.,McDonald, L.,Cygler, M.,Grinstein, S.,Brumell, J.H.
Salmonella Disrupts Host Endocytic Trafficking by SopD2-Mediated Inhibition of Rab7.
Cell Rep, 12:1508-1518, 2015

PubMed Abstract: Intracellular bacterial pathogens of a diverse nature share the ability to evade host immunity by impairing trafficking of endocytic cargo to lysosomes for degradation, a process that is poorly understood. Here, we show that the Salmonella enterica type 3 secreted effector SopD2 mediates this process by binding the host regulatory GTPase Rab7 and inhibiting its nucleotide exchange. Consequently, this limits Rab7 interaction with its dynein- and kinesin-binding effectors RILP and FYCO1 and thereby disrupts host-driven regulation of microtubule motors. Our study identifies a bacterial effector capable of directly binding and thereby modulating Rab7 activity and a mechanism of endocytic trafficking disruption that may provide insight into the pathogenesis of other bacteria. Additionally, we provide a powerful tool for the study of Rab7 function, and a potential therapeutic target.

PubMed: 26299973
DOI: 10.1016/j.celrep.2015.07.063

Experimental method

X-RAY DIFFRACTION (2.15 Å)