Molecular architecture and electrostatic properties of a bacterial porin

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Science  13 Dec 1991:
Vol. 254, Issue 5038, pp. 1627-1630
DOI: 10.1126/science.1721242


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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