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PDBsum entry 3cxb
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Signaling protein
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PDB id
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3cxb
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References listed in PDB file
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Key reference
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Title
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Structure and function of salmonella sifa indicate that its interactions with skip, Ssej, And rhoa family gtpases induce endosomal tubulation.
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Authors
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M.B.Ohlson,
Z.Huang,
N.M.Alto,
M.P.Blanc,
J.E.Dixon,
J.Chai,
S.I.Miller.
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Ref.
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Cell Host Microbe, 2008,
4,
434-446.
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PubMed id
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Abstract
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The Salmonella typhimurium type III secretion effector protein SifA is essential
for inducing tubulation of the Salmonella phagosome and binds the mammalian
kinesin-binding protein SKIP. Coexpression of SifA with the effector SseJ
induced tubulation of mammalian cell endosomes, similar to that induced by
Salmonella infection. Interestingly, GTP-bound RhoA, RhoB, and RhoC also induced
endosomal tubulation when coexpressed with SseJ, indicating that SifA likely
mimics or activates a RhoA family GTPase. The structure of SifA in complex with
the PH domain of SKIP revealed that SifA has two distinct domains; the amino
terminus binds SKIP, and the carboxyl terminus has a fold similar to SopE, a
Salmonella effector with Rho GTPase guanine nucleotide exchange factor activity
(GEF). Similar to GEFs, SifA interacted with GDP-bound RhoA, and purified SseJ
and RhoA formed a protein complex, suggesting that SifA, SKIP, SseJ, and RhoA
family GTPases cooperatively promote host membrane tubulation.
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