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- W2807793918 abstract "Surface layers (S-layers) are two-dimensional, proteinaceous, porous lattices that form the outermost cell envelope component of virtually all archaea and many bacteria. Despite exceptional sequence diversity, S-layer proteins (SLPs) share important characteristics such as their ability to form crystalline sheets punctuated with nano-scale pores, and their propensity for charged amino acids, leading to acidic or basic isoelectric points. However, the precise function of S-layers, or the role of charged SLPs and how they relate to cellular metabolism is unknown. Nano-scale lattices affect the diffusion behavior of low-concentration solutes, even if they are significantly smaller than the pore size. Here, we offer a rationale for charged S-layer proteins in the context of the structural evolution of S-layers. Using the ammonia-oxidizing archaea (AOA) as a model for S-layer geometry, and a 2D electrodiffusion reaction computational framework to simulate diffusion and consumption of the charged solute ammonium (NH4+), we find that the characteristic length scales of nanoporous S-layers elevate the concentration of NH4+ in the pseudo-periplasmic space. Our simulations suggest an evolutionary, mechanistic basis for S-layer charge and shed light on the unique ability of some AOA to oxidize ammonia in environments with nanomolar NH4+ availability, with broad implications for comparisons of ecologically distinct populations." @default.
- W2807793918 created "2018-06-21" @default.
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- W2807793918 date "2018-06-13" @default.
- W2807793918 modified "2023-10-11" @default.
- W2807793918 title "Nutrient transport suggests an evolutionary basis for charged archaeal surface layer proteins" @default.
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- W2807793918 doi "https://doi.org/10.1038/s41396-018-0191-0" @default.
- W2807793918 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6155111" @default.
- W2807793918 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29899515" @default.
- W2807793918 hasPublicationYear "2018" @default.
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