Structural basis for the reversible activation of a Rho protein by the bacterial toxin SopE
Open accessAbstract
The bacterial enteropathogen Salmonella typhimurium employs a type III secretion system to inject bacterial toxins into the host cell cytosol. These toxins transiently activate Rho family GTP-binding protein-dependent signaling cascades to induce cytoskeletal rearrangements. One of these translocated Salmonella toxins, SopE, can activate Cdc42 in a Dbl-like fashion despite its lack of sequence similarity to Dbl-like proteins, the Rho-specific eukaryotic guanine nucleotide exchange factors. To elucidate the mechanism of SopE-mediated guanine nucleotide exchange, we have analyzed the structure of the complex between a catalytic fragment of SopE and Cdc42. SopE binds to and locks the switch I and switch II regions of Cdc42 in a conformation that promotes guanine nucleotide release. This conformation is strikingly similar to that of Rac1 in complex with the eukaryotic Dbl-like exchange factor Tiam1. However, the catalytic domain of SopE has an entirely different architecture from that of Tiam1 and interacts with the switch regions via different amino acids. Therefore, SopE represents the first example of a non-Dbl-like protein capable of inducing guanine nucleotide exchange in Rho family proteins.
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Pathogen proteins can have surfaces that resemble host protein surfaces, allowing them to mimic and compete with host protein interactions.
“Mechanistically, pathogen proteins can have surfaces which resemble those of the host, allowing them to mimic and compete with host protein interactions (Figure 3).”
From AlphaFold, Artificial Intelligence (AI), and Allostery (2022) · cites this paper as [208]
Bacterial toxins or effectors mimicking GEF proteins, such as SopE from Salmonella and MAP from Escherichia coli, can interact with Cdc42 and activate it.
“Bacterial secretes toxins or effectors mimicking the GEF proteins, such as SopE (PDB: 1GZS) from Salmonella208 and MAP (PDB: 3GCG) from Escherichia coli,209 can interact with Cdc42 and activate it.”
From AlphaFold, Artificial Intelligence (AI), and Allostery (2022) · cites this paper as [208]
Human-microbiome protein-protein interactions promote GTPase activation.
“Figure 3 Human–microbiome PPIs promote GTPase activation.”
From AlphaFold, Artificial Intelligence (AI), and Allostery (2022) · cites this paper as [208]
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- Authors
- Buchwald, G., Friebel, A., Galán, J. E., Hardt, W., Wittinghofer, A., & Scheffzek, K.
- Affiliations
- Max Planck Society (DE)
- Max-von-Pettenkofer-Institut für Hygiene und Medizinische Mikrobiologie (DE)
- Yale University (US)
- ETH Zurich (CH)
- Max Planck Institute of Molecular Physiology (DE)
- European Molecular Biology Laboratory (DE)
- Corresponding author
- Wittinghofer, Alfred
- Scheffzek, Klaus
- ORCID
- Hardt, Wolf‐Dietrich
- Venue
- The EMBO Journal
- Published
- 2002-07-01
- Volume
- 21
- Issue
- 13
- Pages
- 3286-3295
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC126081
- OpenAlex
- W2044208802
- Cited by
- 135
- References
- 73
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 1 · 2023: 1 · 2022: 3 · 2021: 2 · 2020: 5 · 2019: 2 · 2018: 1 · 2017: 4 · 2016: 4 · 2015: 2 · 2014: 8 · 2013: 8 · 2012: 7
- FWCI
- 4.06
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- SopE, Cdc42, Rho GTPase activation, guanine nucleotide exchange, type III secretion system, Salmonella typhimurium, bacterial toxins, Tiam1, protein complex structure, cytoskeletal rearrangement, host-pathogen signaling
- MeSH terms
- T-Lymphoma Invasion and Metastasis-inducing Protein 1, Amino Acid Sequence, Bacterial Proteins, Guanosine Diphosphate, Guanosine Triphosphate, Humans, Models, Molecular, Molecular Sequence Data, Protein Conformation, Proteins, Recombinant Fusion Proteins, Salmonella typhimurium, Structure-Activity Relationship, Signal Transduction, Sequence Alignment, Sequence Homology, Amino Acid, Crystallography, X-Ray, Evolution, Molecular, Guanine Nucleotide Exchange Factors, cdc42 GTP-Binding Protein, rac1 GTP-Binding Protein, Protein Interaction Mapping
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