ArticleNature microbiology2017
Type VI secretion TssK baseplate protein exhibits structural similarity with phage receptor-binding proteins and evolved to bind the membrane complex.
Article in Nature microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 56 citations in OpenAlex.
- Genomic characterization of the type VI secretion system in extraintestinal pathogenicMicrobiology spectrum · 2026Article
- The type VI secretion system and associated effector proteins.Nature reviews. Microbiology · 2026Review
- Predicted Structures ofViruses · 2025Article
- Co-Occurrence of Toxic Bloom-Forming CyanobacteriaToxins · 2025Article
- The role of the type VI secretion system in the stress resistance of plant-associated bacteria.Stress biology · 2024Review
- No fitness cost entailed by type VI secretion system synthesis, assembly, contraction, or disassembly in enteroaggregativeJournal of bacteriology · 2023Article
- Killing in the name of: T6SS structure and effector diversity.Microbiology (Reading, England) · 2023Review
- Activity and Crystal Structure of the Adherent-InvasiveInternational journal of molecular sciences · 2023Article
- Soft rot pathogenFrontiers in microbiology · 2023Article
- Type VI Secretion Systems: Environmental and Intra-host Competition of Vibrio cholerae.Advances in experimental medicine and biology · 2023Article
- The Biological and Regulatory Role of Type VI Secretion System ofInfection and drug resistance · 2023Review
- Atomic Structure of IglD Demonstrates Its Role as a Component of the Baseplate Complex of themBio · 2022Article
- Identification and structure of an extracellular contractile injection system from the marine bacterium Algoriphagus machipongonensis.Nature microbiology · 2022Article
- The ecological impact of a bacterial weapon: microbial interactions and the Type VI secretion system.FEMS microbiology reviews · 2021Article
- Article
- A novel stabilization mechanism for the type VI secretion system sheath.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Modular Molecular Weaponry Plays a Key Role in Competition Within an EnvironmentalFrontiers in microbiology · 2021Article
- Structural basis for loading and inhibition of a bacterial T6SS phospholipase effector by the VgrG spike.The EMBO journal · 2020Article
- Conserved and Diverse Traits of Adhesion Devices fromViruses · 2020Review
- Fur-Dam Regulatory Interplay at an Internal Promoter of the Enteroaggregative Escherichia coli Type VI SecretionJournal of bacteriology · 2020Article
Corrections and comments
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Authors and funding
14 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The type VI secretion system (T6SS) is a multiprotein machine widespread in Gram-negative bacteria that delivers toxins into both eukaryotic and prokaryotic cells. The mechanism of action of the T6SS is comparable to that of contractile myophages. The T6SS builds a tail-like structure made of an inner tube wrapped by a sheath, assembled under an extended conformation. Contraction of the sheath propels the inner tube towards the target cell. The T6SS tail is assembled on a platform-the baseplate-which is functionally similar to bacteriophage baseplates. In addition, the baseplate docks the tail to a trans-envelope membrane complex that orients the tail towards the target. Here, we report the crystal structure of TssK, a central component of the T6SS baseplate. We show that TssK is composed of three domains, and establish the contribution of each domain to the interaction with TssK partners. Importantly, this study reveals that the N-terminal domain of TssK is structurally homologous to the shoulder domain of phage receptor-binding proteins, and the C-terminal domain binds the membrane complex. We propose that TssK has conserved the domain of attachment to the virion particle but has evolved the reception domain to use the T6SS membrane complex as receptor.
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