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TitleCradle loop regulates β-barrel pore-formation mechanism of Vibrio cholerae cytolysin.
Journal, issue, pagesStructure, Vol. 34, Issue 1, Page 157-174.e6, Year 2026
Publish dateNov 6, 2025
AuthorsMahendra Singh / Arnab Chatterjee / Ananya Nayak / Prasenjit Naskar / Gurvinder Kaur / Jagannath Mondal / Somnath Dutta / Kausik Chattopadhyay /
PubMed AbstractVibrio cholerae cytolysin (VCC) is a β-barrel pore-forming toxin (β-PFT). The membrane insertion of its pore-forming "pre-stem" motif is the most crucial step in the pore-formation mechanism. In ...Vibrio cholerae cytolysin (VCC) is a β-barrel pore-forming toxin (β-PFT). The membrane insertion of its pore-forming "pre-stem" motif is the most crucial step in the pore-formation mechanism. In the soluble monomeric form, pre-stem remains clamped against the central cytolysin domain by the so-called cradle loop. In the course of oligomeric pore-formation in the target membranes, the cradle loop gets detached from the pre-stem and reorients, thus allowing the pre-stem to extend and insert into the membrane. Here, we show that the specific cradle loop residue(s) play crucial roles in governing the pore-formation mechanism of VCC by establishing decisive interactions with the neighboring structural domains/modules. The alteration of the cradle loop residue, Y194 in particular, compromises the membrane-insertion of the pre-stem, and tends to arrest the membrane-bound toxin in the pre-pore-like oligomeric states. Our study suggests that the native cradle loop architecture, with its intact contacts with the surrounding interaction partners, is essential for VCC pore-formation.
External linksStructure / PubMed:41202807
MethodsEM (single particle)
Resolution3.51 - 6.57 Å
Structure data

EMDB-63070: Pre-pore state (without transmembrane barrel) of Y194A Vibrio cholerae cytolysin mutant in liposome.
Method: EM (single particle) / Resolution: 6.57 Å

EMDB-63073: Pre-pore octameric state of T201A Vibrio cholerae cytolysin mutant in liposome
Method: EM (single particle) / Resolution: 4.76 Å

63083

9lh3

EMDB-63083: Half barrel Pre-pore state of Y194A Vibrio cholerae cytolysin mutant in liposome.
PDB-9lh3: Vibrio cholerae cytolysin cradle loop mutant-Y194A half barrel pre-pore model
Method: EM (single particle) / Resolution: 3.51 Å

63088

9lh7

EMDB-63088, PDB-9lh7:
Pore-like heptameric T201A Vibrio cholerae cytolysin mutant
Method: EM (single particle) / Resolution: 3.76 Å

PDB-9ue9:
Heptameric pore structure of Vibrio cholerae Cytolysin (VCC) embedded in lipid bilayer
Method: ELECTRON MICROSCOPY / Resolution: 4 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • vibrio cholerae (bacteria)
KeywordsTOXIN / Membrane Protein / Heptameric Half-barrel Prepore / VCC mutant / Pore-forming toxin / Heptameric Pore-like / Vibrio cholerae Cytolysin (VCC)

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