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The Alternating Access Transport Mechanism in LacY

Lactose permease of Escherichia coli (LacY) is highly dynamic, and sugar binding causes closing of a large inward-facing cavity with opening of a wide outward-facing hydrophilic cavity. Therefore, lactose/H(+) symport via LacY very likely involves a global conformational change that allows alternati...

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Detalles Bibliográficos
Autores principales: Kaback, H. Ronald, Smirnova, Irina, Kasho, Vladimir, Nie, Yiling, Zhou, Yonggang
Formato: Texto
Lenguaje:English
Publicado: Springer-Verlag 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3030946/
https://www.ncbi.nlm.nih.gov/pubmed/21161516
http://dx.doi.org/10.1007/s00232-010-9327-5
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author Kaback, H. Ronald
Smirnova, Irina
Kasho, Vladimir
Nie, Yiling
Zhou, Yonggang
author_facet Kaback, H. Ronald
Smirnova, Irina
Kasho, Vladimir
Nie, Yiling
Zhou, Yonggang
author_sort Kaback, H. Ronald
collection PubMed
description Lactose permease of Escherichia coli (LacY) is highly dynamic, and sugar binding causes closing of a large inward-facing cavity with opening of a wide outward-facing hydrophilic cavity. Therefore, lactose/H(+) symport via LacY very likely involves a global conformational change that allows alternating access of single sugar- and H(+)-binding sites to either side of the membrane. Here, in honor of Stephan H. White’s seventieth birthday, we review in camera the various biochemical/biophysical approaches that provide experimental evidence for the alternating access mechanism.
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spelling pubmed-30309462011-03-16 The Alternating Access Transport Mechanism in LacY Kaback, H. Ronald Smirnova, Irina Kasho, Vladimir Nie, Yiling Zhou, Yonggang J Membr Biol Article Lactose permease of Escherichia coli (LacY) is highly dynamic, and sugar binding causes closing of a large inward-facing cavity with opening of a wide outward-facing hydrophilic cavity. Therefore, lactose/H(+) symport via LacY very likely involves a global conformational change that allows alternating access of single sugar- and H(+)-binding sites to either side of the membrane. Here, in honor of Stephan H. White’s seventieth birthday, we review in camera the various biochemical/biophysical approaches that provide experimental evidence for the alternating access mechanism. Springer-Verlag 2010-12-16 2011 /pmc/articles/PMC3030946/ /pubmed/21161516 http://dx.doi.org/10.1007/s00232-010-9327-5 Text en © The Author(s) 2010 https://creativecommons.org/licenses/by-nc/4.0/ This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited.
spellingShingle Article
Kaback, H. Ronald
Smirnova, Irina
Kasho, Vladimir
Nie, Yiling
Zhou, Yonggang
The Alternating Access Transport Mechanism in LacY
title The Alternating Access Transport Mechanism in LacY
title_full The Alternating Access Transport Mechanism in LacY
title_fullStr The Alternating Access Transport Mechanism in LacY
title_full_unstemmed The Alternating Access Transport Mechanism in LacY
title_short The Alternating Access Transport Mechanism in LacY
title_sort alternating access transport mechanism in lacy
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3030946/
https://www.ncbi.nlm.nih.gov/pubmed/21161516
http://dx.doi.org/10.1007/s00232-010-9327-5
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