This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1bxw
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1bxw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bxw, resolution 2.5Å" /> '''OUTER MEMBRANE PROTEI...)
Next diff →
Revision as of 09:53, 20 November 2007
|
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
Page seeded by OCA on Tue Nov 20 12:00:39 2007
