ArticleJournal of molecular biology2003
Nucleotide binding induces changes in the oligomeric state and conformation of Sec A in a lipid environment: a small-angle neutron-scattering study.
Article in Journal of molecular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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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
25 citing papers in PubMed, 61 citations in OpenAlex.
- Cardiolipin is required in vivo for the stability of bacterial translocon and optimal membrane protein translocation and insertion.Scientific reports · 2020Article
- SecA-Mediated Protein Translocation through the SecYEG Channel.Microbiology spectrum · 2019Review
- Direct visualization of theScience advances · 2019Article
- Solution Structure of an Intramembrane Aspartyl Protease via Small Angle Neutron Scattering.Biophysical journal · 2018Article
- Biophysical approaches for the study of interactions between molecular chaperones and protein aggregates.Chemical communications (Cambridge, England) · 2015Review
- In Vitro Interaction of the Housekeeping SecA1 with the Accessory SecA2 Protein of Mycobacterium tuberculosis.PloS one · 2015Article
- SecA: a potential antimicrobial target.Future medicinal chemistry · 2015Review
- Analysis of SecA dimerization in solution.Biochemistry · 2014Article
- Mapping of the SecA signal peptide binding site and dimeric interface by using the substituted cysteine accessibility method.Journal of bacteriology · 2013Article
- Small angle neutron scattering for the study of solubilised membrane proteins.The European physical journal. E, Soft matter · 2013Review
- Defining the Escherichia coli SecA dimer interface residues through in vivo site-specific photo-cross-linking.Journal of bacteriology · 2013Article
- The bacterial Sec-translocase: structure and mechanism.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- The use of analytical sedimentation velocity to extract thermodynamic linkage.Biophysical chemistry · 2011Article
- SecA, a remarkable nanomachine.Cellular and molecular life sciences : CMLS · 2011Review
- Energetics of SecA dimerization.Journal of molecular biology · 2011Article
- Ezrin induces long-range interdomain allostery in the scaffolding protein NHERF1.Journal of molecular biology · 2009Article
- SecA, the motor of the secretion machine, binds diverse partners on one interactive surface.Journal of molecular biology · 2008Article
- The active ring-like structure of SecA revealed by electron crystallography: conformational change upon interaction with SecB.Journal of structural biology · 2007Article
- Selective photoaffinity labeling identifies the signal peptide binding domain on SecA.Journal of molecular biology · 2007Article
- Oligomeric states of the SecA and SecYEG core components of the bacterial Sec translocon.Biochimica et biophysica acta · 2007Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
In Escherichia coli, SecA is a large, multifunctional protein that is a vital component of the general protein secretion pathway. In its membrane-bound form it functions as the motor component of the protein translocase, perhaps through successive rounds of membrane insertion and ATP hydrolysis. To understand both the energy conversion process and translocase assembly, we have used contrast-matched, small-angle neutron-scattering (SANS) experiments to examine SecA in small unilamellar vesicles of E.coli phospholipids. In the absence of nucleotide, we observe a dimeric form of SecA with a radius of gyration comparable to that previously observed for SecA in solution. In contrast, the presence of either ADP or a non-hydrolyzable ATP analog induces conversion to a monomeric form. The larger radius of gyration for the ATP-bound relative to the ADP-bound form suggests the former has a more expanded global conformation. This is the first direct structural determination of SecA in a lipid bilayer. The SANS data indicate that nucleotide turnover can function as a switch of conformation of SecA in the membrane in a manner consistent with its proposed role in successive cycles of deep membrane penetration and release with concommitant preprotein insertion.
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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.