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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1993-3-10
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pubmed:abstractText |
Structural changes are central to the mechanism of light-driven proton transport by bacteriorhodopsin, a seven-helix membrane protein. The main intermediate formed upon light absorption is M, which occurs between the proton release and uptake steps of the photocycle. To investigate the structure of the M intermediate, we have carried out electron diffraction studies with two-dimensional crystals of wild-type bacteriorhodopsin and the Asp96-->Gly mutant. The M intermediate was trapped by rapidly freezing the crystals in liquid ethane following illumination with a xenon flash lamp at 5 and 25 degrees C. Here, we present 3.5 A resolution Fourier projection maps of the differences between the M intermediate and the ground state of bacteriorhodopsin. The most prominent structural changes are observed in the vicinity of helices F and G and are localized to the cytoplasmic half of the membrane.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8428572-1182271,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8428572-1522585,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8428572-1650486,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8428572-1784713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8428572-1868827,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8428572-1959632,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8428572-1959640,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8428572-2001671,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8428572-2009355,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8428572-2036368,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8428572-2153966,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8428572-2352280,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8428572-2359127,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8428572-2536166,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8428572-2547788,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8428572-2554293,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8428572-2555165,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8428572-2753899,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8428572-2836382,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8428572-3043536,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8428572-3193246,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8428572-35226,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8428572-3790694,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8428572-3978209
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1-8
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8428572-Amino Acid Sequence,
pubmed-meshheading:8428572-Aspartic Acid,
pubmed-meshheading:8428572-Bacteriorhodopsins,
pubmed-meshheading:8428572-Darkness,
pubmed-meshheading:8428572-Electrons,
pubmed-meshheading:8428572-Fourier Analysis,
pubmed-meshheading:8428572-Glycine,
pubmed-meshheading:8428572-Halobacterium,
pubmed-meshheading:8428572-Light,
pubmed-meshheading:8428572-Mutagenesis, Site-Directed,
pubmed-meshheading:8428572-Protein Conformation,
pubmed-meshheading:8428572-Protein Structure, Secondary,
pubmed-meshheading:8428572-Spectrum Analysis,
pubmed-meshheading:8428572-X-Ray Diffraction
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pubmed:year |
1993
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pubmed:articleTitle |
Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin.
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pubmed:affiliation |
MRC Laboratory of Molecular Biology, Cambridge, UK.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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