Structure of the outer membrane protein A transmembrane domain

The outer membrane protein A of Escherichia coli (OmpA) is an intensely studied example in the field of membrane protein folding. We have determined the structure of the OmpA transmembrane domain consisting of residues 1–171, by X-ray diffraction analysis, to a resolution of 2.5 Å. It consists of a regular, extended eight-stranded ß-barrel and appears to be constructed like an inverse micelle with large water-filled cavities, but does not form a pore. Surprisingly, the cavities seem to be highly conserved during evolution. The structure corroborates the concept that all outer membrane proteins consist of ß-barrels. The structure constitutes a ß-barrel membrane anchor that appears to be the outer membrane equivalent of the single-chain α-helix anchor of the inner membrane.

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