ArticleProtein science : a publication of the Protein Society2002
Electrostatic properties of the anion selective porin Omp32 from Delftia acidovorans and of the arginine cluster of bacterial porins.
Article in Protein science : a publication of the Protein Society, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 29 citations in OpenAlex.
- Multidrug efflux in Gram-negative bacteria: structural modifications in active compounds leading to efflux pump avoidance.npj antimicrobials and resistance · 2024Article
- Design and directed evolution of noncanonical β-stereoselective metalloglycosidases.Nature communications · 2022Article
- Data-Driven Derivation of Molecular Substructures That Enhance Drug Activity in Gram-Negative Bacteria.Journal of medicinal chemistry · 2022Article
- Continuum electrostatic calculations of the pKa of ionizable residues in an ion channel: dynamic vs. static input structure.The European physical journal. E, Soft matter · 2010Article
- Identification of outer membrane proteins of Mycobacterium tuberculosis.Tuberculosis (Edinburgh, Scotland) · 2008Article
- Chemical modification of the bacterial porin OmpF: gain of selectivity by volume reduction.Biophysical journal · 2006Article
- Improved 3D continuum calculations of ion flux through membrane channels.European biophysics journal : EBJ · 2003Article
- Molecular basis of bacterial outer membrane permeability revisited.Microbiology and molecular biology reviews : MMBR · 2003Review
- Multistep mechanism of chloride translocation in a strongly anion-selective porin channel.Biophysical journal · 2003Article
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4 authors at 2 institutions in 2 countries.
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Abstract
The functional properties of the anion-selective porin Omp32 from the bacterium Delftia acidovorans, formerly Comamonas acidovorans, are determined by the particularly narrow channel constriction and the electrostatic field inside and outside the pore. A cluster of arginines (Arg 38, Arg 75, and Arg 133) determines the electrostatic field close to the constriction zone. Stacked amino acids carrying charges are prone to drastic pK(a) shifts. However, optimized calculations of the titration behavior of charged groups, based on the finite-difference Poisson-Boltzmann technique, suggest that all the arginines are charged at physiological pH. Protonation of the clustered arginines is stabilized by one buried glutamate residue (Glu 58), which is strongly interacting with Arg 75 and Arg 38. This functional arrangement of three charged amino acid residues is of general significance because it is found in the constriction zones of all known 16-stranded porins from the alpha-, beta-, and gamma-proteobacteria.
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