1bxw: Difference between revisions

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[[Image:1bxw.~~gif~~|left|200px]]

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~~'''~~OUTER MEMBRANE PROTEIN A (OMPA) TRANSMEMBRANE DOMAIN~~'''~~

===OUTER MEMBRANE PROTEIN A (OMPA) TRANSMEMBRANE DOMAIN===

~~==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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_9808047}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 9808047 is the PubMed ID number.

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==About this Structure==

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[[Category: Outer membrane]]

[[Category: Transmembrane protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 12~~:05:49 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:53:39 2008''

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-[[Image:1bxw.gif|left|200px]]
+{{Seed}}
+[[Image:1bxw.png|left|200px]]
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 {{STRUCTURE_1bxw|  PDB=1bxw  |  SCENE=  }}
-'''OUTER MEMBRANE PROTEIN A (OMPA) TRANSMEMBRANE DOMAIN'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9808047}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9808047 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9808047}}
 ==About this Structure==
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 [[Category: Outer membrane]]
 [[Category: Transmembrane protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:05:49 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:53:39 2008''