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Structural and Functional studies on Membrane Attack Complex / Perforin-like proteins
- Title
- Structural and Functional studies on Membrane Attack Complex / Perforin-like proteins
- Funding
- ARC | Discovery Projects
- Contract (GA) number
- DP0986811
- Start Date
- 2009/01/01
- End Date
- 2011/12/31
- Open Access mandate
- no
- Organizations
- -
- More information
- http://purl.org/au-research/grants/arc/DP0986811
-
A new model for pore formation by cholesterol-dependent cytolysins.
Reboul, Cyril F.; Whisstock, James C.; Dunstone, Michelle A (2014)
Projects: NHMRC | The role of membrane attack complex - perforin like pore foaming proteins in disease and immunity (606471), ARC | Structural and Functional studies on Membrane Attack Complex / Perforin-like proteins (DP0986811), ARC | Membrane Attack Complex / Perforin like proteins in Defence, Attack and Developmental Biology (FF0883418), ARC | ARC Centres of Excellences - Grant ID: CE140100011 (CE140100011), ARC | The mechanism of pore formation by Membrane Attack Complex/Perforin-like proteins (DP120104058)Cholesterol Dependent Cytolysins (CDCs) are important bacterial virulence factors that form large (200–300 Å) membrane embedded pores in target cells. Currently, insights from X-ray crystallography, biophysical and single particle cryo-Electron Microscopy (cryo-EM) experiments suggest that soluble monomers first interact with the membrane surface via a C-terminal Immunoglobulin-like domain (Ig; Domain 4). Membrane bound oligomers then assemble into a prepore oligomeric form, following which t...Conformational Changes during Pore Formation by the Perforin-Related Protein Pleurotolysin
Lukoyanova, Natalya; Kondos, Stephanie C.; Farabella, Irene; Law, Ruby H. P.; Reboul, Cyril F.; Caradoc-Davies, Tom T.; Spicer, Bradley A.; Kleifeld, Oded; Traore, Daouda A. K.; Ekkel, Susan M.; Voskoboinik, Ilia; Trapani, Joseph A.; Hatfaludi, Tamas; Oliver, Katherine; Hotze, Eileen M.;... (2015)
Projects: ARC | Structural and Functional studies on Membrane Attack Complex / Perforin-like proteins (DP0986811), ARC | ARC Centres of Excellences - Grant ID: CE140100011 (CE140100011), ARC | The mechanism of pore formation by Membrane Attack Complex/Perforin-like proteins (DP120104058), EC | MEMBRANEATTACK (294408), WT | Cryo-electron microscopy equipment for structure determination of macromolecular and cellular assemblies. (079605), NIH | Pore Formation by Cholesterol Dependent Cytolysins (2R01AI037657-05), NHMRC | The role of membrane attack complex - perforin like pore foaming proteins in disease and immunity (606471)Membrane attack complex/perforin-like (MACPF) proteins comprise the largest superfamily of pore-forming proteins, playing crucial roles in immunity and pathogenesis. Soluble monomers assemble into large transmembrane pores via conformational transitions that remain to be structurally and mechanistically characterised. Here we present an 11 Å resolution cryo-electron microscopy (cryo-EM) structure of the two-part, fungal toxin Pleurotolysin (Ply), together with crystal structures of both compo...Conformational changes during pore formation by the perforin-related protein pleurotolysin.
Lukoyanova, Natalya; Kondos, S.C.; Farabella, Irene; Law, R.H.P.; Reboul, C. F.; Caradoc-Davies, T.T.; Spicer, B.A.; Kleifeld, O; Traore, D.A.K.; Ekkel, S.M.; Voskoboinik, I.; Trapani, J A; Hatfaludi, T.; Oliver, K.; Hotze, E. M.;... (2015)
Projects: WT | Cryo-electron microscopy equipment for structure determination of macromolecular and cellular assemblies. (079605), EC | MEMBRANEATTACK (294408), ARC | ARC Centres of Excellences - Grant ID: CE140100011 (CE140100011), ARC | Structural and Functional studies on Membrane Attack Complex / Perforin-like proteins (DP0986811), ARC | The mechanism of pore formation by Membrane Attack Complex/Perforin-like proteins (DP120104058), NIH | Pore Formation by Cholesterol Dependent Cytolysins (2R01AI037657-05), NHMRC | The role of membrane attack complex - perforin like pore foaming proteins in disease and immunity (606471)Membrane attack complex/perforin-like (MACPF) proteins comprise the largest superfamily of pore-forming proteins, playing crucial roles in immunity and pathogenesis. Soluble monomers assemble into large transmembrane pores via conformational transitions that remain to be structurally and mechanistically characterised. Here we present an 11 Å resolution cryo-electron microscopy (cryo-EM) structure of the two-part, fungal toxin Pleurotolysin (Ply), together with crystal structures of both compo... -
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