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Modulation of Host Signaling by a Bacterial Mimic

Stebbins, C.Erec, Galán, Jorge E·2000·Molecular Cell

Abstract

Salmonella spp. utilize a specialized protein secretion system to deliver a battery of effector proteins into host cells. Several of these effectors stimulate Cdc42- and Rac1-dependent cytoskeletal changes that promote bacterial internalization. These potentially cytotoxic alterations are rapidly reversed by the effector SptP, a tyrosine phosphatase and GTPase activating protein (GAP) that targets Cdc42 and Rac1. The 2.3 A resolution crystal structure of an SptP-Rac1 transition state complex reveals an unusual GAP architecture that mimics host functional homologs. The phosphatase domain possesses a conserved active site but distinct surface properties. Binding to Rac1 induces a dramatic stabilization in SptP of a four-helix bundle that makes extensive contacts with the Switch I and Switch II regions of the GTPase.

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Metadata

Authors
Stebbins, C. E., & Galán, J. E.
Venue
Molecular Cell
Publisher
Elsevier BV
Published
2000-12
Volume
6
Issue
6
Pages
1449-1460
ISSN
1097-2765
Cited by
160
References
3
Language
en

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Stebbins, C. E., & Galán, J. E. (2000). Modulation of Host Signaling by a Bacterial Mimic. Molecular Cell. https://doi.org/10.1016/s1097-2765(00)00141-6