ArticleProceedings of the National Academy of Sciences of the United States of America2011
Opening the periplasmic cavity in lactose permease is the limiting step for sugar binding.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 40 citations in OpenAlex.
- Structural and functional implications of phase separation of membrane protein LacY in Escherichia coli.Nature communications · 2026Article
- Mechanistic aspects of IPTG (isopropylthio-β-galactoside) transport across the cytoplasmic membrane of Escherichia coli-a rate limiting step in the induction of recombinant protein expression.Journal of industrial microbiology & biotechnology · 2023Article
- Switching off: The phenotypic transition to the uninduced state of the lactose uptake pathway.Biophysical journal · 2022Article
- Optimizing the Substrate Uptake Rate of Solute Carriers.Frontiers in physiology · 2022Article
- Article
- It takes two to tango: The dance of the permease.The Journal of general physiology · 2019Review
- Functionality of membrane proteins overexpressed and purified from E. coli is highly dependent upon the strain.Scientific reports · 2019Article
- Engineered occluded apo-intermediate of LacY.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Uptake dynamics in the Lactose permease (LacY) membrane protein transporter.Scientific reports · 2018Article
- Crystal Structure of a ligand-bound LacY-Nanobody Complex.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- The ins and outs of vesicular monoamine transporters.The Journal of general physiology · 2018Review
- Oversized galactosides as a probe for conformational dynamics in LacY.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- An Asymmetric Conformational Change in LacY.Biochemistry · 2017Article
- Quantification of Detergents Complexed with Membrane Proteins.Scientific reports · 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
- Thermodynamics of Nanobody Binding to Lactose Permease.Biochemistry · 2016Article
- Role of Conserved Gly-Gly Pairs on the Periplasmic Side of LacY.Biochemistry · 2016Article
- Structure of LacY with an α-substituted galactoside: Connecting the binding site to the protonation site.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- 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
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
Abstract
The lactose permease (LacY) catalyzes galactoside/H(+) symport via an alternating access mechanism in which sugar- and H(+)-binding sites in the middle of the molecule are alternatively exposed to either side of the membrane by opening and closing of inward- and outward-facing cavities. The crystal structures of wild-type LacY, as well as accessibility data for the protein in the membrane, provide strong support for a conformation with a tightly closed periplasmic side and an open cytoplasmic side (an inward-facing conformation). In this study, rates of substrate binding were measured by stopped-flow with purified LacY either in detergent or in reconstituted proteoliposomes. Binding rates are compared with rates of sugar-induced opening of the periplasmic pathway obtained by using a recently developed method based on unquenching of Trp fluorescence. A linear dependence of galactoside-binding rates on sugar concentration is observed in detergent, whereas reconstituted LacY binds substrate at a slower rate that is independent of sugar concentration. Rates of opening of the periplasmic cavity with LacY in detergent are independent of substrate concentration and are essentially the same for different galactosidic sugars. The findings demonstrate clearly that reconstituted LacY is oriented physiologically with a closed periplasmic side that limits access of sugar to the binding site. Moreover, opening of the periplasmic cavity is the limiting factor for sugar binding with reconstituted LacY and may be the limiting step in the overall transport reaction.
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Registered trials
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.