ArticleProceedings of the National Academy of Sciences of the United States of America2010
Sugar binding induces the same global conformational change in purified LacY as in the native bacterial membrane.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 34 citations in OpenAlex.
- Solvent accessibility changes in a NaThe Journal of biological chemistry · 2020Article
- The proton electrochemical gradient induces a kinetic asymmetry in the symport cycle of LacY.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- It takes two to tango: The dance of the permease.The Journal of general physiology · 2019Review
- Utilizing Biotinylated Proteins Expressed in Yeast to Visualize DNA-Protein Interactions at the Single-Molecule Level.Frontiers in microbiology · 2017Article
- Crystal structure of a LacY-nanobody complex in a periplasmic-open conformation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Role of Conserved Gly-Gly Pairs on the Periplasmic Side of LacY.Biochemistry · 2016Article
- A chemiosmotic mechanism of symport.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Outward-facing conformers of LacY stabilized by nanobodies.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Real-time conformational changes in LacY.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Galactoside-binding site in LacY.Biochemistry · 2014Article
- Structure of sugar-bound LacY.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- The periplasmic cavity of LacY mutant Cys154→Gly: how open is open?Biochemistry · 2013Article
- Trp replacements for tightly interacting Gly-Gly pairs in LacY stabilize an outward-facing conformation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Proton-coupled dynamics in lactose permease.Structure (London, England : 1993) · 2012Article
- Dynamics of the L-fucose/H+ symporter revealed by fluorescence spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Role of the irreplaceable residues in the LacY alternating access mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Evidence for an intermediate conformational state of LacY.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Lactose permease and the alternating access mechanism.Biochemistry · 2011Article
- Opening the periplasmic cavity in lactose permease is the limiting step for sugar binding.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- An early event in the transport mechanism of LacY protein: interaction between helices V and I.The Journal of biological chemistry · 2011Article
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Authors and funding
2 authors at 1 institution in 2 countries.
Funding
Abstract
Many independent lines of evidence indicate that the lactose permease of Escherichia coli (LacY) is highly dynamic and that sugar binding causes closing of a large inward-facing cavity with opening of a wide outward-facing hydrophilic cavity. Therefore, lactose/H(+) symport catalyzed by 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 (the alternating access model). The x-ray crystal structures of LacY, as well as the majority of spectroscopic studies, use purified protein in detergent micelles. By using site-directed alkylation, we now demonstrate that sugar binding induces virtually the same global conformational change in LacY whether the protein is in the native bacterial membrane or is solubilized and purified in detergent. The results also indicate that the x-ray crystal structure reflects the structure of wild-type LacY in the native membrane in the absence of sugar.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.