ArticleCommunications biology2018
Large conformational changes of a highly dynamic pre-protein binding domain in SecA.
Article in Communications biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The trial behind it
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Who cites it
11 citing papers in PubMed, 17 citations in OpenAlex.
- Benchmarking AI Protein Structure Predictors Reveals a Persistent Bias in Multi-State Proteins.bioRxiv : the preprint server for biology · 2026Article
- AFM observation of protein translocation mediated by one unit of SecYEG-SecA complex.Nature communications · 2025Article
- The Multifunctional Preprotein Binding Domain of SecA.Chembiochem : a European journal of chemical biology · 2024Article
- Plastid Molecular Chaperone HSP90C Interacts with the SecA1 Subunit of Sec Translocase for Thylakoid Protein Transport.Plants (Basel, Switzerland) · 2024Article
- A unifying mechanism for protein transport through the core bacterial Sec machinery.Open biology · 2023Review
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- Trigger factor is a bona fide secretory pathway chaperone that interacts with SecB and the translocase.EMBO reports · 2020Article
- Molecular Mimicry of SecA and Signal Recognition Particle Binding to the Bacterial Ribosome.mBio · 2019Article
- Crosslinking and Reconstitution Approaches to Study Protein Transport.The protein journal · 2019Review
- Protein translocation by the SecA ATPase occurs by a power-stroke mechanism.The EMBO journal · 2019Article
- Omnipresent Maxwell's demons orchestrate information management in living cells.Microbial biotechnology · 2019Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SecA is an essential molecular motor for the translocation of proteins across the membrane via the bacterial Sec secretion system. While the Sec system is found in all cells from archaea to multicellular eukaryotes, the SecA protein is mainly found in bacteria. The mechanism of how the motor protein works on a molecular level is still under dispute but it is well established that SecA binds ATP and uses its hydrolysis for the translocation of substrates. In this work, we addressed the question of which conformational changes the protein might undergo during protein translocation. To this end, we investigated the molecular movements of SecA in the absence or the presence of ATP using single-molecule FRET measurements and in silico normal mode analyses. Our results demonstrate that the pre-protein binding domain of SecA is highly dynamic in the absence of the nucleotide and moves towards the helical wing domain in an ATP-bound state.
Identifiers
What OpenQuestion holds
Registered trials
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.