Secondary Structure of a Channel-forming Protein: Porin from E. Coli Outer Membranes

Overview

Journal EMBO J

Specialties Biotechnology
Molecular Biology

Date 1985 Jun 1

PMID 2992934

Citations 34

Authors

B Kleffel

R M Garavito

W Baumeister

J P Rosenbusch

Affiliations

Soon will be listed here.

Abstract

Porin from Escherichia coli outer membranes has been analysed by high angle diffuse X-ray diffraction, and by attenuated total reflection infrared spectroscopy. These methods demonstrate independently that the majority of the polypeptide backbone is arranged in anti-parallel beta-pleated sheet structure. The average length of the beta-strands, which are oriented nearly normal to the membrane plane, is estimated to be 10-12 residues, independent of the method used. Although the details of strand arrangement (beta-barrels or stacked sheets) are not as yet known, porin represents the first transmembrane protein for which beta-structure has been established unequivocally.

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