PMID:9808047

Citation	Pautsch, A and Schulz, GE (1998) Structure of the outer membrane protein A transmembrane domain. Nat. Struct. Biol. 5:1013-7
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 A. It consists of a regular, extended eight-stranded beta-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 beta-barrels. The structure constitutes a beta-barrel membrane anchor that appears to be the outer membrane equivalent of the single-chain alpha-helix anchor of the inner membrane.
Links	PubMed Online version:10.1038/2983
Keywords	Amino Acid Sequence; Bacterial Outer Membrane Proteins/chemistry; Crystallography, X-Ray; Escherichia coli/chemistry; Lipid Bilayers; Models, Molecular; Molecular Sequence Data; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Homology, Amino Acid
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