ArticleProceedings of the National Academy of Sciences of the United States of America2015
Structure of LacY with an α-substituted galactoside: Connecting the binding site to the protonation site.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- Structure and allostery in major facilitator superfamily symport mechanisms.Acta crystallographica. Section D, Structural biology · 2026Article
- Perspective Approaches to "Trojan Horse" Strategy Development for Combating Bacterial Pathogens.Pharmaceuticals (Basel, Switzerland) · 2026Review
- Structural and functional insights of AmpG in muropeptide transport and multiple β-lactam antibiotics resistance.Nature communications · 2025Article
- Transport mechanism of DgoT, a bacterial homolog of SLC17 organic anion transporters.The EMBO journal · 2024Article
- Utilization of AlphaFold2 to Predict MFS Protein Conformations after Selective Mutation.International journal of molecular sciences · 2022Article
- X-ray crystallography reveals molecular recognition mechanism for sugar binding in a melibiose transporter MelB.Communications biology · 2021Article
- Insights into the Role of the Discontinuous TM7 Helix of Human Ferroportin through the Prism of the Asp325 Residue.International journal of molecular sciences · 2021Article
- Function Trumps Form in Two Sugar Symporters,International journal of molecular sciences · 2021Review
- Structure and mechanism of a redesigned multidrug transporter from the Major Facilitator Superfamily.Scientific reports · 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
- Article
- It takes two to tango: The dance of the permease.The Journal of general physiology · 2019Review
- Structures suggest a mechanism for energy coupling by a family of organic anion transporters.PLoS biology · 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
- Oversized galactosides as a probe for conformational dynamics in LacY.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Functional Characterization of the Saccharomyces cerevisiae Equilibrative Nucleoside Transporter 1 (ScENT1).Molecules (Basel, Switzerland) · 2018Article
- Proton movement and coupling in the POT family of peptide transporters.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Ferrous iron efflux systems in bacteria.Metallomics : integrated biometal science · 2017Review
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4 authors.
Funding
Abstract
The X-ray crystal structure of a conformationally constrained mutant of the Escherichia coli lactose permease (the LacY double-Trp mutant Gly-46→Trp/Gly-262→Trp) with bound p-nitrophenyl-α-d-galactopyranoside (α-NPG), a high-affinity lactose analog, is described. With the exception of Glu-126 (helix IV), side chains Trp-151 (helix V), Glu-269 (helix VIII), Arg-144 (helix V), His-322 (helix X), and Asn-272 (helix VIII) interact directly with the galactopyranosyl ring of α-NPG to provide specificity, as indicated by biochemical studies and shown directly by X-ray crystallography. In contrast, Phe-20, Met-23, and Phe-27 (helix I) are within van der Waals distance of the benzyl moiety of the analog and thereby increase binding affinity nonspecifically. Thus, the specificity of LacY for sugar is determined solely by side-chain interactions with the galactopyranosyl ring, whereas affinity is increased by nonspecific hydrophobic interactions with the anomeric substituent.
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