ArticleStructure (London, England : 1993)2014
NMR polypeptide backbone conformation of the E. coli outer membrane protein W.
Article in Structure (London, England : 1993), 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, 36 citations in OpenAlex.
- Solution NMR Spectroscopy for the Determination of Structures of Membrane Proteins in a Lipid Environment.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Immunodominant extracellular loops of Treponema pallidum FadL outer membrane proteins elicit antibodies with opsonic and growth-inhibitory activities.PLoS pathogens · 2024Article
- Immunodominant extracellular loops ofbioRxiv : the preprint server for biology · 2024Article
- Gating of β-Barrel Protein Pores, Porins, and Channels: An Old Problem with New Facets.International journal of molecular sciences · 2023Review
- Article
- An engineered construct of cFLIP provides insight into DED1 structure and interactions.Structure (London, England : 1993) · 2022Article
- Lipid Membrane Mimetics in Functional and Structural Studies of Integral Membrane Proteins.Membranes · 2021Review
- Structural Modeling of the Treponema pallidum Outer Membrane Protein Repertoire: a Road Map for Deconvolution of Syphilis Pathogenesis and Development of a Syphilis Vaccine.Journal of bacteriology · 2021Article
- Comparative analysis ofJournal of biomolecular NMR · 2021Article
- A β-barrel for oil transport through lipid membranes: Dynamic NMR structures of AlkL.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy.Angewandte Chemie (International ed. in English) · 2020Article
- Backbone Hydrogen Bond Energies in Membrane Proteins Are Insensitive to Large Changes in Local Water Concentration.Journal of the American Chemical Society · 2020Article
- Spotlight on the Ballet of Proteins: The Structural Dynamic Properties of Proteins Illuminated by Solution NMR.International journal of molecular sciences · 2020Review
- Article
- Building Blocks of the Outer Membrane: Calculating a General Elastic Energy Model for β-Barrel Membrane Proteins.Journal of chemical theory and computation · 2018Article
- Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.Chemical reviews · 2018Review
- Comparison of NMR and crystal structures of membrane proteins and computational refinement to improve model quality.Proteins · 2018Article
- Transcriptional Regulation of the Outer Membrane Porin Gene ompW Reveals its Physiological Role during the Transition from the Aerobic to the Anaerobic Lifestyle of Escherichia coli.Frontiers in microbiology · 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
- Micro-scale NMR Experiments for Monitoring the Optimization of Membrane Protein Solutions for Structural Biology.Bio-protocol · 2015Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The outer membrane proteins (Omps) are key factors for bacterial survival and virulence. Among the Omps that have been structurally characterized either by X-ray crystallography or by NMR in solution, the crystal structure of OmpW stands out because three of its four extracellular loops are well defined, whereas long extracellular loops in other E. coli Omps are disordered in the crystals as well as in NMR structures. OmpW thus presented an opportunity for a detailed comparison of the extracellular loops in a β-barrel membrane protein structure in crystals and in noncrystalline milieus. Here, the polypeptide backbone conformation of OmpW in 30-Fos micelles was determined. Complete backbone NMR assignments were obtained and the loops were structurally characterized. In combination with the OmpW crystal structure, NMR line shape analyses, and (15)N{(1)H}-NOE data, these results showed that intact regular secondary structures in the loops undergo slow hinge motions at the detergent-solvent interface.
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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.