ArticleStructure (London, England : 1993)2013
The glove-like structure of the conserved membrane protein TatC provides insight into signal sequence recognition in twin-arginine translocation.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed.
- Structure and substrate recognition by the bacterial twin-arginine translocation (Tat) core complex.Nature microbiology · 2026Article
- Tat-dependent protein translocation and its evolution.FEMS microbiology reviews · 2026Review
- The mechanism of Tat-dependent protein translocation.Microbial cell (Graz, Austria) · 2026Article
- The Transmembrane Glutamate Serves as a pH Sensor for Tha4 Oligomerization During Twin Arginine Transport of Proteins.Plants (Basel, Switzerland) · 2025Article
- A larger TatBC complex associates with TatA clusters for transport of folded proteins across the bacterial cytoplasmic membrane.Scientific reports · 2024Article
- Identification of novel small molecule inhibitors of twin arginine translocation (Tat) pathway and their effect on the control ofFrontiers in microbiology · 2024Article
- Length matters: Functional flip of the short TatA transmembrane helix.Biophysical journal · 2023Article
- Characterization of a TatA/TatB binding site on the TatC component of theMicrobiology (Reading, England) · 2023Article
- Bcs1, a novel target for fungicide.Frontiers in chemistry · 2023Review
- New insights into the Tat protein transport cycle from characterizing the assembled Tat translocon.Molecular microbiology · 2022Article
- Occurrence and potential mechanism of holin-mediated non-lytic protein translocation in bacteria.Microbial cell (Graz, Austria) · 2022Review
- Oligomerization state of the functional bacterial twin-arginine translocation (Tat) receptor complex.Communications biology · 2022Article
- What have molecular simulations contributed to understanding of Gram-negative bacterial cell envelopes?Microbiology (Reading, England) · 2022Review
- Bacterial Signal Peptides- Navigating the Journey of Proteins.Frontiers in physiology · 2022Review
- Translocation of Proteins through a Distorted Lipid Bilayer.Trends in cell biology · 2021Review
- Influence of the TorD signal peptide chaperone on Tat-dependent protein translocation.PloS one · 2021Article
- Genome-Wide Identification and Bioinformatics Characterization of Superoxide Dismutases in the Desiccation-Tolerant CyanobacteriumFrontiers in microbiology · 2021Article
- Article
- Targeting of proteins to the twin-arginine translocation pathway.Molecular microbiology · 2020Review
- Structural basis of ER-associated protein degradation mediated by the Hrd1 ubiquitin ligase complex.Science (New York, N.Y.) · 2020Article
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4 authors.
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Abstract
In bacteria, two signal-sequence-dependent secretion pathways translocate proteins across the cytoplasmic membrane. Although the mechanism of the ubiquitous general secretory pathway is becoming well understood, that of the twin-arginine translocation pathway, responsible for translocation of folded proteins across the bilayer, is more mysterious. TatC, the largest and most conserved of three integral membrane components, provides the initial binding site of the signal sequence prior to pore assembly. Here, we present two crystal structures of TatC from the thermophilic bacteria Aquifex aeolicus at 4.0 Å and 6.8 Å resolution. The membrane architecture of TatC includes a glove-shaped structure with a lipid-exposed pocket predicted by molecular dynamics to distort the membrane. Correlating the biochemical literature to these results suggests that the signal sequence binds in this pocket, leading to structural changes that facilitate higher order assemblies.
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