PDBsum entry 5cpc

Cell invasion

PDB id: 5cpc

Contents

Protein chains

281 a.a.

Waters ×109

PDB id:

5cpc

Name:

Cell invasion

Title:

Crystal structure of sopd, a type iii secreted virulence effector from salmonella enterica

Structure:

Secreted effector protein sopd. Chain: a, b. Synonym: salmonella outer protein d. Engineered: yes

Source:

Salmonella typhimurium (strain lt2 / sgsc1412 / atcc 700720). Organism_taxid: 99287. Strain: lt2 / sgsc1412 / atcc 700720. Gene: sopd, stm2945. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.15Å R-factor: 0.214 R-free: 0.243

Authors:

R.Shi,M.Cygler,Montreal-Kingston Bacterial Structural Genomics Initiative (Bsgi)

Key ref:

V.M.D'Costa et al. (2015). Salmonella Disrupts Host Endocytic Trafficking by SopD2-Mediated Inhibition of Rab7. Cell Rep, 12, 1508-1518. PubMed id: 26299973 DOI: 10.1016/j.celrep.2015.07.063

Date:

21-Jul-15 Release date: 09-Sep-15

Protein chains

P40722  (SOPD_SALTY) -  Secreted effector protein SopD from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

Seq: 317 a.a.

Struc: 281 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.celrep.2015.07.063

Cell Rep 12:1508-1518 (2015)

PubMed id: 26299973

Salmonella Disrupts Host Endocytic Trafficking by SopD2-Mediated Inhibition of Rab7.

V.M.D'Costa, V.Braun, M.Landekic, R.Shi, A.Proteau, L.McDonald, M.Cygler, S.Grinstein, J.H.Brumell.

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.