ArticleJournal of the American Chemical Society2013
NMR-based conformational ensembles explain pH-gated opening and closing of OmpG channel.
Article in Journal of the American Chemical Society, 2013. 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, 35 citations in OpenAlex.
- Barrel expansion of outer membrane protein G nanopore through β-hairpin duplication.Protein science : a publication of the Protein Society · 2025Article
- Gating of β-Barrel Protein Pores, Porins, and Channels: An Old Problem with New Facets.International journal of molecular sciences · 2023Review
- An Engineered OmpG Nanopore with Displayed Peptide Motifs for Single-Molecule Multiplex Protein Detection.Angewandte Chemie (International ed. in English) · 2023Article
- Correlation of membrane protein conformational and functional dynamics.Nature communications · 2021Article
- A pH-independent quiet OmpG pore with enhanced electrostatic repulsion among the extracellular loops.Biochimica et biophysica acta. Biomembranes · 2021Article
- Spotlight on the Ballet of Proteins: The Structural Dynamic Properties of Proteins Illuminated by Solution NMR.International journal of molecular sciences · 2020Review
- Computational design of structured loops for new protein functions.Biological chemistry · 2019Review
- Mechanism of OmpG pH-Dependent Gating from Loop Ensemble and Single Channel Studies.Journal of the American Chemical Society · 2018Article
- Structure of outer membrane protein G in lipid bilayers.Nature communications · 2017Article
- Engineering a Novel Porin OmpGF Via Strand Replacement from Computational Analysis of Sequence Motif.Biochimica et biophysica acta. Biomembranes · 2017Article
- NMR as a tool to investigate the structure, dynamics and function of membrane proteins.Nature structural & molecular biology · 2016Article
- A functional NMR for membrane proteins: dynamics, ligand binding, and allosteric modulation.Protein science : a publication of the Protein Society · 2016Review
- In Silico Structure and Sequence Analysis of Bacterial Porins and Specific Diffusion Channels for Hydrophilic Molecules: Conservation, Multimericity and Multifunctionality.International journal of molecular sciences · 2016Article
- OprG Harnesses the Dynamics of its Extracellular Loops to Transport Small Amino Acids across the Outer Membrane of Pseudomonas aeruginosa.Structure (London, England : 1993) · 2015Article
- Selective Detection of Protein Homologues in Serum Using an OmpG Nanopore.Analytical chemistry · 2015Article
- Electrostatic Interactions between OmpG Nanopore and Analyte Protein Surface Can Distinguish between Glycosylated Isoforms.The journal of physical chemistry. B · 2015Article
- Article
- Visualizing transient dark states by NMR spectroscopy.Quarterly reviews of biophysics · 2015Article
- NMR polypeptide backbone conformation of the E. coli outer membrane protein W.Structure (London, England : 1993) · 2014Article
- Control of the conductance of engineered protein nanopores through concerted loop motions.Angewandte Chemie (International ed. in English) · 2014Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The outer membrane protein G (OmpG) is a monomeric 33 kDa 14-stranded β-barrel membrane protein functioning as a nonspecific porin for the uptake of oligosaccharides in Escherichia coli. Two different crystal structures of OmpG obtained at different values of pH suggest a pH-gated pore opening mechanism. In these structures, extracellular loop 6 extends away from the barrel wall at neutral pH but is folded back into the pore lumen at low pH, blocking transport through the pore. Loop 6 was invisible in a previously published solution NMR structure of OmpG in n-dodecylphosphocholine micelles, presumably due to conformational exchange on an intermediate NMR time scale. Here we present an NMR paramagnetic relaxation enhancement (PRE)-based approach to visualize the conformational dynamics of loop 6 and to calculate conformational ensembles that explain the pH-gated opening and closing of the OmpG channel. The different loop conformers detected by the PRE ensemble calculations were validated by disulfide cross-linking of strategically engineered cysteines and electrophysiological single channel recordings. The results indicate a more dynamically regulated channel opening and closing than previously thought and reveal additional membrane-associated conformational ensembles at pH 6.3 and 7.0. We anticipate this approach to be generally applicable to detect and characterize functionally important conformational ensembles of membrane proteins.
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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.