1bxw
From Proteopedia
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'''OUTER MEMBRANE PROTEIN A (OMPA) TRANSMEMBRANE DOMAIN''' | '''OUTER MEMBRANE PROTEIN A (OMPA) TRANSMEMBRANE DOMAIN''' | ||
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[[Category: Pautsch, A.]] | [[Category: Pautsch, A.]] | ||
[[Category: Schulz, G E.]] | [[Category: Schulz, G E.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:05:49 2008'' | |
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Revision as of 09:05, 2 May 2008
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. 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 Page seeded by OCA on Fri May 2 12:05:49 2008
