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TitleStepwise visualization of membrane pore formation by suilysin, a bacterial cholesterol-dependent cytolysin.
Journal, issue, pagesElife, Vol. 3, Page e04247, Year 2014
Publish dateDec 2, 2014
AuthorsCarl Leung / Natalya V Dudkina / Natalya Lukoyanova / Adrian W Hodel / Irene Farabella / Arun P Pandurangan / Nasrin Jahan / Mafalda Pires Damaso / Dino Osmanović / Cyril F Reboul / Michelle A Dunstone / Peter W Andrew / Rana Lonnen / Maya Topf / Helen R Saibil / Bart W Hoogenboom /
PubMed AbstractMembrane attack complex/perforin/cholesterol-dependent cytolysin (MACPF/CDC) proteins constitute a major superfamily of pore-forming proteins that act as bacterial virulence factors and effectors in ...Membrane attack complex/perforin/cholesterol-dependent cytolysin (MACPF/CDC) proteins constitute a major superfamily of pore-forming proteins that act as bacterial virulence factors and effectors in immune defence. Upon binding to the membrane, they convert from the soluble monomeric form to oligomeric, membrane-inserted pores. Using real-time atomic force microscopy (AFM), electron microscopy (EM), and atomic structure fitting, we have mapped the structure and assembly pathways of a bacterial CDC in unprecedented detail and accuracy, focussing on suilysin from Streptococcus suis. We show that suilysin assembly is a noncooperative process that is terminated before the protein inserts into the membrane. The resulting ring-shaped pores and kinetically trapped arc-shaped assemblies are all seen to perforate the membrane, as also visible by the ejection of its lipids. Membrane insertion requires a concerted conformational change of the monomeric subunits, with a marked expansion in pore diameter due to large changes in subunit structure and packing.
External linksElife / PubMed:25457051 / PubMed Central
MethodsEM (single particle)
Resolution15.0 Å
Structure data

EMDB-2979:
Cryo EM structure of suilysin prepore
Method: EM (single particle) / Resolution: 15.0 Å

EMDB-2983:
Cryo EM structure of suilysin pore
Method: EM (single particle) / Resolution: 15.0 Å

Source
  • Streptococcus suis (bacteria)

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