ArticleJournal of structural biology2009
Structure-function relationships of the outer membrane translocon Wza investigated by cryo-electron microscopy and mutagenesis.
Article in Journal of structural biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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.
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.
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Who cites it
9 citing papers in PubMed.
- Multiple extracellular polymeric substance pathways transcribed byApplied and environmental microbiology · 2025Article
- Development and mechanism exploration of a quantitative model for Escherichia coli transformation efficiency based on ultrasonic power.Ultrasonics sonochemistry · 2024Article
- The making of hypervirulent Klebsiella pneumoniae.Journal of clinical laboratory analysis · 2022Review
- Bacterial Outer Membrane Polysaccharide Export (OPX) Proteins Occupy Three Structural Classes with Selective β-Barrel Porin Requirements for Polymer Secretion.Microbiology spectrum · 2022Article
- Structural features underlying recognition and translocation of extracellular polysaccharides.Interface focus · 2019Review
- Review
- Outer membrane lipoprotein biogenesis: Lol is not the end.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015Review
- Trapped translocation intermediates establish the route for export of capsular polysaccharides across Escherichia coli outer membranes.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Bacterial polymers: biosynthesis, modifications and applications.Nature reviews. Microbiology · 2010Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
The outer membrane protein Wza, from Escherichia coli K30, forms an octameric complex that is essential for capsular polysaccharide export. Homologs of Wza are widespread in gram-negative bacterial pathogens where capsules are critical virulence determinants. Wza is unusual in that it spans the outer membrane using a barrel composed of amphipathic alpha-helices, rather than being a beta-barrel like almost all other outer membrane channels. The transmembrane helical barrel of Wza also forms the external opening to a hydrophilic translocation pathway that spans the periplasm. Here, we have probed the structure and function of the Wza complex using both cryo-electron microscopy and mutagenesis. The helical barrel structure is stable in detergent micelles under mildly acidic conditions but is destabilized at basic pH, although the overall quaternary structure is retained. Truncation of the C-terminal region that forms the helical barrel by 4 residues has no effect on the ability of Wza to oligomerize and support capsule export, but larger truncations of 18, 24 or 35 amino acids abolish its function. The bulk of the C-terminal domain is essential for the stability and assembly of the E. coli Wza complex.
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Registered trials
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