ArticleScientific reports2015
Crystal structure of a COG4313 outer membrane channel.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
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- Uptake of monoaromatic hydrocarbons during biodegradation by FadL channel-mediated lateral diffusion.Nature communications · 2020Article
- Antibiotic susceptibility signatures identify potential antimicrobial targets in the Acinetobacter baumannii cell envelope.Nature communications · 2020Article
- MbnH is a diheme MauG-like protein associated with microbial copper homeostasis.The Journal of biological chemistry · 2019Article
- Comparative Genomic Analysis of the Regulation of Aromatic Metabolism in Betaproteobacteria.Frontiers in microbiology · 2019Article
- Ecology and Biogenesis of Functional Amyloids in Pseudomonas.Journal of molecular biology · 2018Review
- Indole Biodegradation in Acinetobacter sp. Strain O153: Genetic and Biochemical Characterization.Applied and environmental microbiology · 2017Article
- A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis.Nature communications · 2017Article
- Metabolic pathway for a new strain Pseudomonas synxantha LSH-7': from chemotaxis to uptake of n-hexadecane.Scientific reports · 2017Article
- Discovery of Novel Leptospirosis Vaccine Candidates Using Reverse and Structural Vaccinology.Frontiers in immunology · 2017Article
- Purification, crystallization and characterization of the Pseudomonas outer membrane protein FapF, a functional amyloid transporter.Acta crystallographica. Section F, Structural biology communications · 2016Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
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Abstract
COG4313 proteins form a large and widespread family of outer membrane channels and have been implicated in the uptake of a variety of hydrophobic molecules. Structure-function studies of this protein family have so far been hampered by a lack of structural information. Here we present the X-ray crystal structure of Pput2725 from the biodegrader Pseudomonas putida F1, a COG4313 channel of unknown function, using data to 2.3 Å resolution. The structure shows a 12-stranded barrel with an N-terminal segment preceding the first β-strand occluding the lumen of the barrel. Single channel electrophysiology and liposome swelling experiments suggest that while the narrow channel visible in the crystal structure does allow passage of ions and certain small molecules in vitro, Pput2725 is unlikely to function as a channel for hydrophilic molecules. Instead, the presence of bound detergent molecules inside the barrel suggests that Pput2725 mediates uptake of hydrophobic molecules. Sequence alignments and the locations of highly conserved residues suggest the presence of a dynamic lateral opening through which hydrophobic molecules might gain entry into the cell. Our results provide the basis for structure-function studies of COG4313 family members with known function, such as the SphA sphingosine uptake channel of Pseudomonas aeruginosa.
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