ArticleProceedings of the National Academy of Sciences of the United States of America2007
Site-directed alkylation and the alternating access model for LacY.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
88 citing papers in PubMed, 144 citations in OpenAlex.
- General principles of secondary active transporter function.Biophysics reviews · 2022Review
- Solvent accessibility changes in a NaThe Journal of biological chemistry · 2020Article
- Plant glucose transporter structure and function.Pflugers Archiv : European journal of physiology · 2020Review
- Article
- Site-Directed Alkylation Detected by In-Gel Fluorescence (SDAF) to Determine the Topology Map and Probe the Solvent Accessibility of Membrane Proteins.Scientific reports · 2019Article
- 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
- Free Energy Landscape of the Complete Transport Cycle in a Key Bacterial Transporter.ACS central science · 2018Article
- Structural elements required for coupling ion and substrate transport in the neurotransmitter transporter homolog LeuT.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
- Oversized galactosides as a probe for conformational dynamics in LacY.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Topological Dissection of the Membrane Transport Protein Mhp1 Derived from Cysteine Accessibility and Mass Spectrometry.Analytical chemistry · 2017Article
- An Asymmetric Conformational Change in LacY.Biochemistry · 2017Article
- Crystal Structure and Conformational Change Mechanism of a Bacterial Nramp-Family Divalent Metal Transporter.Structure (London, England : 1993) · 2016Article
- 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
- Formation of a Chloride-conducting State in the Maltose ATP-binding Cassette (ABC) Transporter.The Journal of biological chemistry · 2016Article
- Andrew A. Benson: personal recollections.Photosynthesis research · 2016Article
- The Structure and Function of OxlT, the Oxalate Transporter of Oxalobacter formigenes.The Journal of membrane biology · 2015Review
- ATP binding drives substrate capture in an ECF transporter by a release-and-catch mechanism.Nature structural & molecular biology · 2015Article
28 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 1 institution in 2 countries.
Funding
Abstract
In a functional lactose permease mutant from Escherichia coli (LacY) devoid of native Cys residues, almost every residue was replaced individually with Cys and tested for reactivity with the permeant alkylating agent N-ethylmaleimide in right-side-out membrane vesicles. Here we present the results in the context of the crystal structure of LacY. Engineered Cys replacements located near or within the inward-facing hydrophilic cavity or at other solvent-accessible positions in LacY react well with this alkylating agent. Cys residues facing the low dielectric of the membrane or located in tightly packed regions of the structure react poorly. Remarkably, in the presence of ligand, increased reactivity is observed with Cys replacements located predominantly on the periplasmic side of the sugar-binding site. In contrast, other Cys replacements largely on the cytoplasmic side of the binding site exhibit decreased reactivity. Furthermore, both sets of Cys replacements in the putative cavities are located at the periplasmic (increased reactivity) and cytoplasmic (decreased reactivity) ends of the same helices and distributed in a pseudosymmetrical manner. The results are consistent with a model in which the single sugar-binding site in the approximate middle of the molecule is alternately exposed to either side of the membrane due to opening and closing of cytoplasmic and periplasmic hydrophilic cavities.
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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.