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1bxw

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(New page: 200px<br /><applet load="1bxw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bxw, resolution 2.5&Aring;" /> '''OUTER MEMBRANE PROTEI...)
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[[Image:1bxw.gif|left|200px]]<br /><applet load="1bxw" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1bxw, resolution 2.5&Aring;" />
caption="1bxw, resolution 2.5&Aring;" />
'''OUTER MEMBRANE PROTEIN A (OMPA) TRANSMEMBRANE DOMAIN'''<br />
'''OUTER MEMBRANE PROTEIN A (OMPA) TRANSMEMBRANE DOMAIN'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1BXW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with C8E as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BXW OCA].
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1BXW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=C8E:'>C8E</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BXW OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Pautsch, A.]]
[[Category: Pautsch, A.]]
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[[Category: Schulz, G.E.]]
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[[Category: Schulz, G E.]]
[[Category: C8E]]
[[Category: C8E]]
[[Category: outer membrane]]
[[Category: outer membrane]]
[[Category: transmembrane protein]]
[[Category: transmembrane protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:00:39 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:00:17 2008''

Revision as of 10:00, 21 February 2008

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 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 Thu Feb 21 12:00:17 2008

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