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Title | Single-particle cryo-EM reveals conformational variability of the oligomeric VCC β-barrel pore in a lipid bilayer. |
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Journal, issue, pages | J Cell Biol, Vol. 220, Issue 12, Year 2021 |
Publish date | Dec 6, 2021 |
Authors | Nayanika Sengupta / Anish Kumar Mondal / Suman Mishra / Kausik Chattopadhyay / Somnath Dutta / |
PubMed Abstract | Vibrio cholerae cytolysin (VCC) is a water-soluble, membrane-damaging, pore-forming toxin (PFT) secreted by pathogenic V. cholerae, which causes eukaryotic cell death by altering the plasma membrane ...Vibrio cholerae cytolysin (VCC) is a water-soluble, membrane-damaging, pore-forming toxin (PFT) secreted by pathogenic V. cholerae, which causes eukaryotic cell death by altering the plasma membrane permeability. VCC self-assembles on the cell surface and undergoes a dramatic conformational change from prepore to heptameric pore structure. Over the past few years, several high-resolution structures of detergent-solubilized PFTs have been characterized. However, high-resolution structural characterization of small β-PFTs in a lipid environment is still rare. Therefore, we used single-particle cryo-EM to characterize the structure of the VCC oligomer in large unilamellar vesicles, which is the first atomic-resolution cryo-EM structure of VCC. From our study, we were able to provide the first documented visualization of the rim domain amino acid residues of VCC interacting with lipid membrane. Furthermore, cryo-EM characterization of lipid bilayer-embedded VCC suggests interesting conformational variabilities, especially in the transmembrane channel, which could have a potential impact on the pore architecture and assist us in understanding the pore formation mechanism. |
External links | J Cell Biol / PubMed:34617964 / PubMed Central |
Methods | EM (single particle) |
Resolution | 4.0 - 5.6 Å |
Structure data | EMDB-31972: EMDB-31973: EMDB-31974: |
Source |
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