The S-component fold: a link between bacterial transporters and receptors
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Abstract
The processes of nutrient uptake and signal sensing are crucial for microbial survival and adaptation. Membrane-embedded proteins involved in these functions (transporters and receptors) are commonly regarded as unrelated in terms of sequence, structure, mechanism of action and evolutionary history. Here, we analyze the protein structural universe using recently developed artificial intelligence-based structure prediction tools, and find an unexpected link between prominent groups of microbial transporters and receptors. The so-called S-components of Energy-Coupling Factor (ECF) transporters, and the membrane domains of sensor histidine kinases of the 5TMR cluster share a structural fold. The discovery of their relatedness manifests a widespread case of prokaryotic “transceptors” (related proteins with transport or receptor function), showcases how artificial intelligence-based structure predictions reveal unchartered evolutionary connections between proteins, and provides new avenues for engineering transport and signaling functions in bacteria.
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Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
Ins and outs of AlphaFold2 transmembrane protein structure predictions
Hegedűs, T., Geisler, M., Lukács, G. L., & Farkas, B. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-04112-1 · Cited by 127 · see citing works
Structure and mechanism of the S component of a bacterial ECF transporter
Zhang, P., Wang, J., & Shi, Y. (2010) · Nature · doi:10.1038/nature09488 · Cited by 99 · see citing works
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- Authors
- Partipilo, M., & Slotboom, D. J.
- Affiliations
- University of Groningen (NL)
- Corresponding author
- Slotboom, Dirk Jan
- Venue
- Communications Biology
- Published
- 2024-05-21
- Volume
- 7
- Issue
- 1
- Pages
- 610-610
- ISSN
- 2399-3642 (ISSN-L)
- PMC
- PMC11109136
- OpenAlex
- W4398173255
- Cited by
- 4
- References
- 3
- Citations by year
- 2025: 2 · 2024: 2
- FWCI
- 0.54
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Communications Biology (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- University of Groningen research database (University of Groningen / Centre for Information Technology) (publishedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek (714.018.003.)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- sensor histidine kinase, transceptors, bacterial membrane transporters, bacterial receptors, protein structural evolution, nutrient uptake, signal sensing
- MeSH terms
- Histidine Kinase, Artificial Intelligence, Bacteria, Bacterial Proteins, Models, Molecular, Signal Transduction, Protein Folding, Membrane Transport Proteins
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