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1bxw

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Image:1bxw.gif

1bxw, resolution 2.5Å

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OUTER MEMBRANE PROTEIN A (OMPA) TRANSMEMBRANE DOMAIN

Overview

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.

About this Structure

1BXW is a Single protein structure of sequence from Escherichia coli with C8E as ligand. Full crystallographic information is available from OCA.

Reference

Structure of the outer membrane protein A transmembrane domain., Pautsch A, Schulz GE, Nat Struct Biol. 1998 Nov;5(11):1013-7. PMID:9808047

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