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Structure of the outer membrane protein A transmembrane domain

Nature Structural Biology volume 5, pages 1013–1017 (1998)Cite this article

Abstract

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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Figure 1: Structure of the OmpA transmembrane domain.
Figure 2
Figure 3: Topology sketch of OmpA171 as viewed from the barrel exterior.
Figure 4: Stereoviews of the internal architecture of OmpA171.
Figure 5: Sequence alignment of the transmembrane domain of the outer membrane protein A of E. coli (OmpA171 numbering) with five homologues found with FASTA in the EMBL Data Bank.

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Acknowledgements

We thank U. Henning for providing us with the gene of OmpA171 and K. Model and C. Siebold for essential contributions during crystal production. The project was supported by the Sonderforschungsbereich-428.

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  1. Institut für Organische Chemie und Biochemie, Albert-Ludwigs-Universität, Albertstrasse 21, Freiburg im Breisgau, D-79104, Germany

    Alex Pautsch & Georg E. Schulz

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Pautsch, A., Schulz, G. Structure of the outer membrane protein A transmembrane domain. Nat Struct Mol Biol 5, 1013–1017 (1998). https://doi.org/10.1038/2983

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