ArticleCell reports2012
Structure of the SecY complex unlocked by a preprotein mimic.
Article in Cell reports, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
45 citing papers in PubMed.
- Microbial membrane transport genes in maize rhizosphere under fertilization - a preliminary study.Scientific reports · 2026Article
- Dynamic coupling of fast channel gating with slow ATP-turnover underpins protein transport through the Sec translocon.The EMBO journal · 2024Article
- A unifying mechanism for protein transport through the core bacterial Sec machinery.Open biology · 2023Review
- Forty years in cryoEM of membrane proteins.Microscopy (Oxford, England) · 2022Article
- Characterization of the Features of Water Inside the SecY Translocon.The Journal of membrane biology · 2021Review
- Stepwise gating of the Sec61 protein-conducting channel by Sec63 and Sec62.Nature structural & molecular biology · 2021Article
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- Refined measurement of SecA-driven protein secretion reveals that translocation is indirectly coupled to ATP turnover.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- SecY-mediated quality control prevents the translocation of non-gated porins.Scientific reports · 2020Article
- Article
- SecA-Mediated Protein Translocation through the SecYEG Channel.Microbiology spectrum · 2019Review
- A molecular dynamics study on the resilience of Sec61 channel from open to closed state.RSC advances · 2019Article
- ATP-induced asymmetric pre-protein folding as a driver of protein translocation through the Sec machinery.eLife · 2019Article
- The Dynamic ATP-Driven Mechanism of Bacterial Protein Translocation and the Critical Role of Phospholipids.Frontiers in microbiology · 2019Review
- Specific cardiolipin-SecY interactions are required for proton-motive force stimulation of protein secretion.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Dynamic action of the Sec machinery during initiation, protein translocation and termination.eLife · 2018Article
- The way is the goal: how SecA transports proteins across the cytoplasmic membrane in bacteria.FEMS microbiology letters · 2018Review
- The interaction network of the YidC insertase with the SecYEG translocon, SRP and the SRP receptor FtsY.Scientific reports · 2018Article
- The Sec System: Protein Export inEcoSal Plus · 2017Review
- Alignment of the protein substrate hairpin along the SecA two-helix finger primes protein transport inProceedings of the National Academy of Sciences of the United States of America · 2017Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
The Sec complex forms the core of a conserved machinery coordinating the passage of proteins across or into biological membranes. The bacterial complex SecYEG interacts with the ATPase SecA or translating ribosomes to translocate secretory and membrane proteins accordingly. A truncated preprotein competes with the physiological full-length substrate and primes the protein-channel complex for transport. We have employed electron cryomicroscopy of two-dimensional crystals to determine the structure of the complex unlocked by the preprotein. Its visualization in the native environment of the membrane preserves the active arrangement of SecYEG dimers, in which only one of the two channels is occupied by the polypeptide substrate. The signal sequence could be identified along with the corresponding conformational changes in SecY, including relocation of transmembrane segments 2b and 7 as well as the plug, which presumably then promote channel opening. Therefore, we propose that the structure describes the translocon unlocked by preprotein and poised for protein translocation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.