ArticlePloS one2017
An evolutionarily conserved glycine-tyrosine motif forms a folding core in outer membrane proteins.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Sequence Conservation and Functional Significance of Charged Clusters in Mitochondria-Located Proteins of Green Plants.Journal of molecular evolution · 2026Article
- Mutations affecting the β-sheet at the extracellular opening of the intimin β-barrel domain lead to reduced protein levels and inefficient passenger secretion.Bioscience reports · 2026Article
- Probing the Dynamics of Yersinia Adhesin A (YadA) in Outer Membranes Hints at Requirements for β-Barrel Membrane Insertion.Journal of the American Chemical Society · 2025Article
- Sculpting conducting nanopore size and shape through de novo protein design.Science (New York, N.Y.) · 2024Article
- Rationale in Custom Design of Transmembrane β-Barrel Pores.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Sculpting conducting nanopore size and shape throughbioRxiv : the preprint server for biology · 2023Article
- Identification of the Keratin-Associated Protein 22-2 Gene in theAnimals : an open access journal from MDPI · 2023Article
- Architecture and autoinhibitory mechanism of the plasma membrane NaNature communications · 2023Article
- The Role of Extracellular Loops in the Folding of Outer Membrane Protein X (OmpX) ofFrontiers in molecular biosciences · 2022Article
- Inward-facing glycine residues create sharp turns in β-barrel membrane proteins.Biochimica et biophysica acta. Biomembranes · 2021Article
- Outer membrane protein evolution.Current opinion in structural biology · 2021Review
- De novo design of transmembrane β barrels.Science (New York, N.Y.) · 2021Article
- Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients.Nature communications · 2020Article
- Biomimetic Membranes with Transmembrane Proteins: State-of-the-Art in Transmembrane Protein Applications.International journal of molecular sciences · 2019Review
- Outer Membrane Protein Insertion by the β-barrel Assembly Machine.EcoSal Plus · 2019Review
- Ecology and Biogenesis of Functional Amyloids in Pseudomonas.Journal of molecular biology · 2018Review
- Article
- Diversity and motif conservation in protein 3D structural landscape: exploration by a new multivariate simulation method.Journal of molecular modeling · 2018Article
- Outer membrane protein folding from an energy landscape perspective.BMC biology · 2017Review
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6 authors.
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No grant is acknowledged in the PubMed record.
Abstract
An intimate interaction between a pair of amino acids, a tyrosine and glycine on neighboring β-strands, has been previously reported to be important for the structural stability of autotransporters. Here, we show that the conservation of this interacting pair extends to nearly all major families of outer membrane β-barrel proteins, which are thought to have originated through duplication events involving an ancestral ββ hairpin. We analyzed the function of this motif using the prototypical outer membrane protein OmpX. Stopped-flow fluorescence shows that two folding processes occur in the millisecond time regime, the rates of which are reduced in the tyrosine mutant. Folding assays further demonstrate a reduction in the yield of folded protein for the mutant compared to the wild-type, as well as a reduction in thermal stability. Taken together, our data support the idea of an evolutionarily conserved 'folding core' that affects the folding, membrane insertion, and thermal stability of outer membrane protein β-barrels.
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