ArticleThe EMBO journal2001
Projection structure and oligomeric properties of a bacterial core protein translocase.
Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 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
49 citing papers in PubMed.
- Dynamic coupling of fast channel gating with slow ATP-turnover underpins protein transport through the Sec translocon.The EMBO journal · 2024Article
- Interaction of the periplasmic chaperone SurA with the inner membrane protein secretion (SEC) machinery.The Biochemical journal · 2023Article
- Cell-Free Expression to Probe Co-Translational Insertion of an Alpha Helical Membrane Protein.Frontiers in molecular biosciences · 2022Article
- Role of Transportome in the Gills of Chinese Mitten Crabs in Response to Salinity Change: A Meta-Analysis of RNA-Seq Datasets.Biology · 2021Article
- Comparison of Single and Multiple Turnovers of SecYEG in Escherichia coli.Journal of bacteriology · 2020Article
- Inter-membrane association of the Sec and BAM translocons for bacterial outer-membrane biogenesis.eLife · 2020Article
- Article
- ATP-induced asymmetric pre-protein folding as a driver of protein translocation through the Sec machinery.eLife · 2019Article
- 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
- Penetration into membrane of amino-terminal region of SecA when associated with SecYEG in active complexes.Protein science : a publication of the Protein Society · 2018Article
- Each protomer of a dimeric YidC functions as a single membrane insertase.Scientific reports · 2018Article
- Article
- Composition and Activity of the Non-canonical Gram-positive SecY2 Complex.The Journal of biological chemistry · 2016Article
- Membrane protein insertion and assembly by the bacterial holo-translocon SecYEG-SecDF-YajC-YidC.The Biochemical journal · 2016Article
- Unlocking the Bacterial SecY Translocon.Structure (London, England : 1993) · 2016Article
- Escherichia coli SecG is required for residual export mediated by mutant signal sequences and for SecY-SecE complex stability.Journal of bacteriology · 2015Article
- Membrane protein insertion and proton-motive-force-dependent secretion through the bacterial holo-translocon SecYEG-SecDF-YajC-YidC.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Specificity of SecYEG for PhoA precursors and SecA homologs on SecA protein-conducting channels.Biochemical and biophysical research communications · 2013Article
- Two copies of the SecY channel and acidic lipids are necessary to activate the SecA translocation ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Promiscuous targeting of polytopic membrane proteins to SecYEG or YidC by the Escherichia coli signal recognition particle.Molecular biology of the cell · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The major route for protein export or membrane integration in bacteria occurs via the Sec-dependent transport apparatus. The core complex in the inner membrane, consisting of SecYEG, forms a protein-conducting channel, while the ATPase SecA drives translocation of substrate across the membrane. The SecYEG complex from Escherichia coli was overexpressed, purified and crystallized in two dimensions. A 9 A projection structure was calculated using electron cryo-microscopy. The structure exhibits P12(1) symmetry, having two asymmetric units inverted with respect to one another in the unit cell. The map shows elements of secondary structure that appear to be transmembrane helices. The crystallized form of SecYEG is too small to comprise the translocation channel and does not contain a large pore seen in other studies. In detergent solution, the SecYEG complex displays an equilibrium between monomeric and tetrameric forms. Our results therefore indicate that, unlike other known channels, the SecYEG complex can exist as both an assembled channel and an unassembled smaller unit, suggesting that transitions between the two states occur during a functional cycle.
Indexed as
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.