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Biochim Biophys Acta. 2012 Nov;1818(11):2908-16. doi: 10.1016/j.bbamem.2012.07.009. Epub 2012 Jul 21.

Cation selectivity is a conserved feature in the OccD subfamily of Pseudomonas aeruginosa.

Author information

1
Department of Physics, Syracuse University, Syracuse, NY 13244-1130, USA.

Abstract

To achieve the uptake of small, water-soluble nutrients, Pseudomonas aeruginosa, a pathogenic Gram-negative bacterium, employs substrate-specific channels located within its outer membrane. In this paper, we present a detailed description of the single-channel characteristics of six members of the outer membrane carboxylate channel D (OccD) subfamily. Recent structural studies showed that the OccD proteins share common features, such as a closely related, monomeric, 18-stranded β-barrel conformation and large extracellular loops, which are folded back into the channel lumen. Here, we report that the OccD proteins displayed single-channel activity with a unitary conductance covering an unusually broad range, between 20 and 670pS, as well as a diverse gating dynamics. Interestingly, we found that cation selectivity is a conserved trait among all members of the OccD subfamily, bringing a new distinction between the members of the OccD subfamily and the anion-selective OccK channels. Conserved cation selectivity of the OccD channels is in accord with an increased specificity and selectivity of these proteins for positively charged, carboxylate-containing substrates.

PMID:
22824298
PMCID:
PMC3424372
DOI:
10.1016/j.bbamem.2012.07.009
[Indexed for MEDLINE]
Free PMC Article

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