The topography of the purple membrane View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1979-04

AUTHORS

JOHN E. WALKER, ALEXANDER F. CARNE, HERBERT W. SCHMITT

ABSTRACT

THE purple membrane of Halobacterium halobium functions as a light-driven proton pump1,2. It is about 45 Å thick3 and contains a single polypeptide chain comprising about 240 amino acids4. Retinal is covalently attached to a specific lysine residue4 and has been implicated in the absorption of incident light energy2. The retinal lies at an angle of about 20° to the plane of the bilayer5. Seven protein rods running through the membrane, probably α-helices, have been detected by electron diffraction6,7. Circular dichroism studies indicate a 75% helical content which is consistent with a seven-helix model8. A structure containing seven such α-helices requires about 210 amino acids to cross a membrane 45 Å thick seven times, thus implying that most of the polypeptide chain is buried in the lipid bilayer. Digestion of the membrane with proteolytic enzymes supports this view and only three parts of the polypeptide chain are apparently exposed. Here, we show by sequence analysis of digestion products that a section corresponding to the N-terminal seven residues is removed by pronase and proteinase K. More... »

PAGES

653-654

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/278653a0

DOI

http://dx.doi.org/10.1038/278653a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1014408569

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/450067


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