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Science 13 December 1991:
Vol. 254. no. 5038, pp. 1627 - 1630
DOI: 10.1126/science.1721242
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Articles

Science, Vol 254, Issue 5038, 1627-1630
Copyright © 1991 by American Association for the Advancement of Science

articles

Molecular architecture and electrostatic properties of a bacterial porin

MS Weiss, U Abele, J Weckesser, W Welte, E Schiltz, and GE Schulz

Institut fur Organische Chemie und Biochemie, Freiburg, Federal Republic of Germany.

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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