ArticleJournal of structural biology2007
The active ring-like structure of SecA revealed by electron crystallography: conformational change upon interaction with SecB.
Article in Journal of structural biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
12 citing papers in PubMed.
- β-Barrel Assembly Machinery (BAM) Complex as Novel Antibacterial Drug Target.Molecules (Basel, Switzerland) · 2023Review
- SecA inhibitors as potential antimicrobial agents: differential actions on SecA-only and SecA-SecYEG protein-conducting channels.FEMS microbiology letters · 2018Review
- Article
- SecA: a potential antimicrobial target.Future medicinal chemistry · 2015Review
- Prediction of lipid-binding regions in cytoplasmic and extracellular loops of membrane proteins as exemplified by protein translocation membrane proteins.The Journal of membrane biology · 2013Article
- Article
- Escherichia coli membranes depleted of SecYEG elicit SecA-dependent ion-channel activity but lose signal peptide specificity.The Journal of membrane biology · 2012Article
- SecA alone can promote protein translocation and ion channel activity: SecYEG increases efficiency and signal peptide specificity.The Journal of biological chemistry · 2011Article
- SecA, a remarkable nanomachine.Cellular and molecular life sciences : CMLS · 2011Review
- Protein secretion and outer membrane assembly in Alphaproteobacteria.FEMS microbiology reviews · 2008Review
- Full-length Escherichia coli SecA dimerizes in a closed conformation in solution as determined by cryo-electron microscopy.The Journal of biological chemistry · 2008Article
- Effects of SecE depletion on the inner and outer membrane proteomes of Escherichia coli.Journal of bacteriology · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
SecA is a multifunctional protein involved in protein translocation in bacteria. The structure of SecA on membrane is dramatically altered compared with that in solution, accompanying with functional changes. We previously reported the formation of a novel ring-like structure of SecA on lipid layers, which may constitute part of the preprotein translocation channel. In the present work, two-dimensional crystallization of Escherichia coli SecA on lipid monolayers was performed to reveal the structural details of SecA on lipid layers and to investigate its function. The 2D crystals composed of ring-like structures were obtained by specific interaction between SecA and negatively charged lipid. The 2D projection map and 3D reconstruction from negative stained 2D crystals exhibited a distinct open channel-like structure of SecA, with an outer diameter of 7 nm and an inner diameter of 2 nm, providing the structural evidence for SecA importance in forming the part of the translocation channel. This pore structure is altered after transferring crystals to the SecB solution, indicating that the lipid-specific SecA structure has the SecB binding activity. The strategy developed here provides a promising technique for studying structure of SecA complex with its ligand on membrane.
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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.