ArticleInternational journal of molecular sciences2016
In Silico Structure and Sequence Analysis of Bacterial Porins and Specific Diffusion Channels for Hydrophilic Molecules: Conservation, Multimericity and Multifunctionality.
Article in International journal of molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Topology and functional characterization of major outer membrane proteins of Treponema maltophilum and Treponema lecithinolyticum.Molecular oral microbiology · 2025Article
- Composition and in situ structure of theScience advances · 2024Article
- Entropy and Variability: A Second Opinion by Deep Learning.Biomolecules · 2022Article
- Metal(loid) speciation and transformation by aerobic methanotrophs.Microbiome · 2021Review
- Structural insights into the main S-layer unit ofThe Journal of biological chemistry · 2020Article
- Article
- Crystal structure of the outer membrane protein OmpU from Vibrio cholerae at 2.2 Å resolution.Acta crystallographica. Section D, Structural biology · 2018Article
- Outer membrane phospholipase A's roles inGut pathogens · 2017Article
Corrections and comments
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Authors and funding
4 authors.
Funding
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Abstract
Diffusion channels are involved in the selective uptake of nutrients and form the largest outer membrane protein (OMP) family in Gram-negative bacteria. Differences in pore size and amino acid composition contribute to the specificity. Structure-based multiple sequence alignments shed light on the structure-function relations for all eight subclasses. Entropy-variability analysis results are correlated to known structural and functional aspects, such as structural integrity, multimericity, specificity and biological niche adaptation. The high mutation rate in their surface-exposed loops is likely an important mechanism for host immune system evasion. Multiple sequence alignments for each subclass revealed conserved residue positions that are involved in substrate recognition and specificity. An analysis of monomeric protein channels revealed particular sequence patterns of amino acids that were observed in other classes at multimeric interfaces. This adds to the emerging evidence that all members of the family exist in a multimeric state. Our findings are important for understanding the role of members of this family in a wide range of bacterial processes, including bacterial food uptake, survival and adaptation mechanisms.
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Registered trials
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