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Updated: Jul 12, 2026

Electron Cryotomography of Bacterial Cells
Published on: May 6, 2010
Molecular architecture and electrostatic properties of a bacterial porin
M S Weiss1, U Abele, J Weckesser
1Institut für Organische Chemie und Biochemie, Freiburg, Federal Republic of Germany.
Abstract:
The integral membrane protein porin from Rhodobacter capsulatus consists of three tightly associated 16-stranded beta barrels that give rise to three distinct diffusion channels for small solutes through the outer membrane. The x-ray structure of this porin has revealed details of its shape, the residue distributions within the pore and at the membrane-facing surface, and the location of calcium sites. The electrostatic potential has been calculated and related to function. Moreover, potential calculations were found to predict the Ca2+ sites.
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