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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...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Springer-Verlag
2010
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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. |
format | Text |
id | pubmed-3030946 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Springer-Verlag |
record_format | MEDLINE/PubMed |
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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