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In silico structure and sequence analysis of bacterial porins and specific diffusion channels for hydrophilic molecules: Conservation, multimericity and multifunctionality

International Journal of Molecular Sciences, ISSN: 1422-0067, Vol: 17, Issue: 4, Page: 599
2016
  • 15
    Citations
  • 0
    Usage
  • 31
    Captures
  • 0
    Mentions
  • 203
    Social Media
Metric Options:   Counts1 Year3 Year

Metrics Details

  • Citations
    15
  • Captures
    31
  • Social Media
    203
    • Shares, Likes & Comments
      203
      • Facebook
        203

Article Description

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.

Bibliographic Details

Vollan, Hilde S; Tannæs, Tone; Vriend, Gert; Bukholm, Geir

MDPI AG

Chemical Engineering; Biochemistry, Genetics and Molecular Biology; Chemistry; Computer Science

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