ArticleProceedings of the National Academy of Sciences of the United States of America2014
Outward-facing conformers of LacY stabilized by nanobodies.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 24 citations in OpenAlex.
- Nanobody-mediated control of long RSH Rel and RelA catalysis by restriction of their conformational landscape.Nature communications · 2026Article
- Trimbody with rigid AI-designed scaffolds enables atomic-resolution cryo-EM structure determination of small proteins.Nature communications · 2026Article
- Structural and functional insights of AmpG in muropeptide transport and multiple β-lactam antibiotics resistance.Nature communications · 2025Article
- Cryo-EM structure of antibacterial efflux transporter QacA from Staphylococcus aureus reveals a novel extracellular loop with allosteric role.The EMBO journal · 2023Article
- Review
- Plant glucose transporter structure and function.Pflugers Archiv : European journal of physiology · 2020Review
- Article
- Functional Expression of the Human Glucose Transporters GLUT2 and GLUT3 in Yeast Offers Novel Screening Systems for GLUT-Targeting Drugs.Frontiers in molecular biosciences · 2020Article
- It takes two to tango: The dance of the permease.The Journal of general physiology · 2019Review
- Engineered occluded apo-intermediate of LacY.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Crystal Structure of a ligand-bound LacY-Nanobody Complex.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Isolation of state-dependent monoclonal antibodies against the 12-transmembrane domain glucose transporter 4 using virus-like particles.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- 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 artificial transport metabolon facilitates improved substrate utilization in yeast.Nature chemical biology · 2017Article
- An Asymmetric Conformational Change in LacY.Biochemistry · 2017Article
- Nanobodies to Study G Protein-Coupled Receptor Structure and Function.Annual review of pharmacology and toxicology · 2017Review
- 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
- Hxt13, Hxt15, Hxt16 and Hxt17 from Saccharomyces cerevisiae represent a novel type of polyol transporters.Scientific reports · 2016Article
- Transient conformers of LacY are trapped by nanobodies.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 4 countries.
Funding
Abstract
The lactose permease of Escherichia coli (LacY), a highly dynamic polytopic membrane protein, catalyzes stoichiometric galactoside/H(+) symport by an alternating access mechanism and exhibits multiple conformations, the distribution of which is altered by sugar binding. We have developed single-domain camelid nanobodies (Nbs) against a LacY mutant in an outward (periplasmic)-open conformation to stabilize this state of the WT protein. Twelve purified Nbs inhibit lactose transport in right-side-out membrane vesicles, indicating that the Nbs recognize epitopes on the periplasmic side of LacY. Stopped-flow kinetics of sugar binding by WT LacY in detergent micelles or reconstituted into proteoliposomes reveals dramatic increases in galactoside-binding rates induced by interaction with the Nbs. Thus, WT LacY in complex with the great majority of the Nbs exhibits varied increases in access of sugar to the binding site with an increase in association rate constants (kon) of up to ∼ 50-fold (reaching 10(7) M(-1) ⋅ s(-1)). In contrast, with the double-Trp mutant, which is already open on the periplasmic side, the Nbs have little effect. The findings are clearly consistent with stabilization of WT conformers with an open periplasmic cavity. Remarkably, some Nbs drastically decrease the rate of dissociation of bound sugar leading to increased affinity (greater than 200-fold for lactose).
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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.