ArticleBiochimica et biophysica acta. Biomembranes2021
Inward-facing glycine residues create sharp turns in β-barrel membrane proteins.
Article in Biochimica et biophysica acta. Biomembranes, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 9 citations in OpenAlex.
- Molecular insights into the inhibition of MexCD-OprJ efflux pumps by menthol and thymol in Pseudomonas aeruginosa.Antonie van Leeuwenhoek · 2025Article
- Seeing is believing: Illuminating the Gram-negative outer membrane with molecular dynamics simulations.Current opinion in structural biology · 2024Review
- Evolutionary Engineering a Larger Porin Using a Loop-to-Hairpin Mechanism.Journal of molecular biology · 2023Article
- Evolutionary engineering a larger porin using a loop-to-hairpin mechanism.bioRxiv : the preprint server for biology · 2023Article
- Conformational dynamics and putative substrate extrusion pathways of the N-glycosylated outer membrane factor CmeC from Campylobacter jejuni.PLoS computational biology · 2023Article
- Modeling intermediates of BamA folding an outer membrane protein.Biophysical journal · 2022Article
- Automated Cardiac Chamber Size and Cardiac Physiology Measurement in Water Fleas by U-Net and Mask RCNN Convolutional Networks.Animals : an open access journal from MDPI · 2022Article
- The Role of Extracellular Loops in the Folding of Outer Membrane Protein X (OmpX) ofFrontiers in molecular biosciences · 2022Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The transmembrane region of outer-membrane proteins (OMPs) of Gram-negative bacteria are almost exclusively β-barrels composed of between 8 and 26 β-strands. To explore the relationship between β-barrel size and shape, we modeled and simulated engineered variants of the Escherichia coli protein OmpX with 8, 10, 12, 14, and 16 β-strands. We found that while smaller barrels maintained a roughly circular shape, the 16-stranded variant developed a flattened cross section. This flat cross section impeded its ability to conduct ions, in agreement with previous experimental observations. Flattening was determined to arise from the presence of inward-facing glycines at sharp turns in the β-barrel. An analysis of all simulations revealed that glycines, on average, make significantly smaller angles with residues on neighboring strands than all other amino acids, including alanine, and create sharp turns in β-barrel cross sections. This observation was generalized to 119 unique structurally resolved OMPs. We also found that the fraction of glycines in β-barrels decreases as the strand number increases, suggesting an evolutionary role for the addition or removal of glycine in OMP sequences.
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