ArticleJournal of molecular biology2015
Conformational Changes of the Clamp of the Protein Translocation ATPase SecA.
Article in Journal of molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 27 citations in OpenAlex.
- Stepwise accumulation of SecA mutations enables high-stringency azide-based selection in Escherichia coli.The Journal of antibiotics · 2026Article
- Benchmarking AI Protein Structure Predictors Reveals a Persistent Bias in Multi-State Proteins.bioRxiv : the preprint server for biology · 2026Article
- A unifying mechanism for protein transport through the core bacterial Sec machinery.Open biology · 2023Review
- Structural basis of SecA-mediated protein translocation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Molecular dynamics of DNA translocation by FtsK.Nucleic acids research · 2022Article
- Article
- Protease protection assays show polypeptide movement into the SecY channel by power strokes of the SecA ATPase.EMBO reports · 2020Article
- The Structure ofInternational journal of molecular sciences · 2020Article
- Novel Sequence Feature of SecA Translocase Protein Unique to the Thermophilic Bacteria: Bioinformatics Analyses to Investigate Their Potential Roles.Microorganisms · 2019Article
- SecA-Mediated Protein Translocation through the SecYEG Channel.Microbiology spectrum · 2019Review
- Structure of the substrate-engaged SecA-SecY protein translocation machine.Nature communications · 2019Article
- Article
- Protein translocation by the SecA ATPase occurs by a power-stroke mechanism.The EMBO journal · 2019Article
- Single-molecule observation of nucleotide induced conformational changes in basal SecA-ATP hydrolysis.Science advances · 2018Article
- The way is the goal: how SecA transports proteins across the cytoplasmic membrane in bacteria.FEMS microbiology letters · 2018Review
- The Sec System: Protein Export inEcoSal Plus · 2017Review
- Preprotein mature domains contain translocase targeting signals that are essential for secretion.The Journal of cell biology · 2017Article
- Protein export through the bacterial Sec pathway.Nature reviews. Microbiology · 2017Review
- Structural Similarities and Differences between Two Functionally Distinct SecA Proteins, Mycobacterium tuberculosis SecA1 and SecA2.Journal of bacteriology · 2015Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Post-translational protein translocation across the bacterial plasma membrane is mediated by the interplay of the SecA ATPase and the protein-conducting SecY channel. SecA consists of several domains, including two nucleotide-binding domains (NBD1 and NBD2), a polypeptide cross-linking domain (PPXD), a helical scaffold domain (HSD), and a helical wing domain (HWD). PPXD, HSD, and NBD2 form a clamp that positions the polypeptide substrate above the channel so that it can be pushed into the channel by a two-helix finger of the HSD. How the substrate is accommodated in the clamp during translocation is unclear. Here, we report a crystal structure of Thermotoga maritima SecA at 1.9 Å resolution. Structural analysis and free-energy calculations indicate that the new structure represents an intermediate state during the transition of the clamp from an open to a closed conformation. Molecular dynamics simulations show that closure of the clamp occurs in two phases, an initial movement of PPXD, HSD, and HWD as a unit, followed by a movement of PPXD alone toward NBD2. Simulations in the presence of a polypeptide chain show that the substrate associates with the back of the clamp by dynamic hydrogen bonding and that the clamp is laterally closed by a conserved loop of the PPXD. Mutational disruption of clamp opening or closure abolishes protein translocation. These results suggest how conformational changes of SecA allow substrate binding and movement during protein translocation.
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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.