ArticleNature communications2018
Structural basis for chitin acquisition by marine Vibrio species.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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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Who cites it
22 citing papers in PubMed, 55 citations in OpenAlex.
- Structure-based classification of bacterial chitooligosaccharide-specific outer membrane porins (ChiPs).The Journal of biological chemistry · 2026Article
- Performance of Nitrogen Removal and Biofilm-Associated Microbial Community in a Compact Marine Shrimp Recirculating Aquaculture System with MBBR.Microorganisms · 2026Article
- Streptomyces venezuelae uses secreted chitinases and a designated ABC transporter to support the competitive saprophytic catabolism of chitin.PLoS biology · 2025Article
- A suite of ddPCR assays targeting microbial pathogens for improved management of shellfish aquaculture.Applied and environmental microbiology · 2025Article
- Functional genomics of chitin degradation by Vibrio parahaemolyticus reveals finely integrated metabolic contributions to support environmental fitness.PLoS genetics · 2025Article
- Conformational flexibility driving charge-selective substrate translocation across a bacterial transporter.Chemical science · 2024Article
- Complete genome sequence of a winter seasonMicrobial genomics · 2024Article
- Periplasmic chitooligosaccharide-binding protein requires a three-domain organization for substrate translocation.Scientific reports · 2023Article
- Inherited chitinases enable sustained growth and rapid dispersal of bacteria from chitin particles.Nature microbiology · 2023Article
- Shell disease syndromes of decapod crustaceans.Environmental microbiology · 2023Review
- Article
- Recognition of discrete export signals in early flagellar subunits during bacterial type III secretion.eLife · 2022Article
- The C2 entity of chitosugars is crucial in molecular selectivity of the Vibrio campbellii chitoporin.The Journal of biological chemistry · 2021Article
- Inward-facing glycine residues create sharp turns in β-barrel membrane proteins.Biochimica et biophysica acta. Biomembranes · 2021Article
- Probing the physiological roles of the extracellular loops of chitoporin from Vibrio campbellii.Biophysical journal · 2021Article
- Mucin Glycans Signal through the Sensor Kinase RetS to Inhibit Virulence-Associated Traits in Pseudomonas aeruginosa.Current biology : CB · 2021Article
- Chitoporin from Serratia marcescens: recombinant expression, purification and crystallization.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Role of the lipid bilayer in outer membrane protein folding in Gram-negative bacteria.The Journal of biological chemistry · 2020Review
- Single-channel properties, sugar specificity, and role of chitoporin in adaptive survival ofThe Journal of biological chemistry · 2020Article
- Membrane directed expression in Escherichia coli of BBA57 and other virulence factors from the Lyme disease agent Borrelia burgdorferi.Scientific reports · 2019Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chitin, an insoluble polymer of N-acetylglucosamine, is one of the most abundant biopolymers on Earth. By degrading chitin, chitinolytic bacteria such as Vibrio harveyi are critical for chitin recycling and maintenance of carbon and nitrogen cycles in the world's oceans. A decisive step in chitin degradation is the uptake of chito-oligosaccharides by an outer membrane protein channel named chitoporin (ChiP). Here, we report X-ray crystal structures of ChiP from V. harveyi in the presence and absence of chito-oligosaccharides. Structures without bound sugar reveal a trimeric assembly with an unprecedented closing of the transport pore by the N-terminus of a neighboring subunit. Substrate binding ejects the pore plug to open the transport channel. Together with molecular dynamics simulations, electrophysiology and in vitro transport assays our data provide an explanation for the exceptional affinity of ChiP for chito-oligosaccharides and point to an important role of the N-terminal gate in substrate transport.
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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.