Structural basis of pore formation by cholesterol-binding toxins

International Journal of Medical Microbiology

Volumn 290, Issue 4-5, 2000, Pages 389-394

  Gilbert, Robert J C ^a,b   Jimenez, Josá L ^c   Chen, Shaoxia ^c   Andrew, Peter W ^d   Saibil, Helen R ^c  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c UNIVERSITY OF LONDON   (United Kingdom)

^d UNIVERSITY OF LEICESTER   (United Kingdom)

Author keywords

3 dimensional electron density maps; Cholesterol binding toxins; Pneumolysin

Indexed keywords

EID: 0033735462     PISSN: 14384221     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1438-4221(00)80049-1     Document Type: Article

References (27)

1. Amino acid changes affecting the activity of pneumolysin alter the behaviour of pneumococci in pneumonia
2. Toxin structure: Part of a hole?
3. Staphylococcal α-hemolysin can form hexamers in phospholipid bilayers
4. An extensively modified version of Molscript that includes greatly enhanced coloring capabilities
5. Self-interaction of pneumolysin, the pore-forming protein toxin of Streptococcus pneumoniae
6. Two structural transitions in membrane pore formation by pneumolysin, the pore-forming toxin of Streptococcus pneumoniae
7. Studies on the structure and mechanism of a bacterial protein toxin by analytical ultracentrifugation and small-angle neutron scattering
8. Kinetic aspects of the aggregation of Clostridium perfringens θ-toxin on erythrocyte membranes
9. Experimental evidence for hydrophobic matching and membrane-mediated interactions in lipid bilayers containing gramicidin
10. Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane α-helical peptides: Importance of hydrophobic mismatch and proposed role of tryptophans
11. Molscript - A program to produce both detailed and schematic plots of protein structures
12. Raster3d version-2.0 - A program for photorealistic molecular graphics
13. Subunit organization and symmetry of pore-forming oligomeric pneumolysin
14. Thiol-activated cytolysins
15. Contribution of tryptophan residues to the structural changes in perfringolysin O during interaction with liposomal membranes
16. The projection structure of perfringolysin O (Clostridium perfringens θ-toxin)
17. Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel
18. Membrane-penetrating domain of streptolysin O identified by cysteine scanning mutagenesis
19. Assembly mechanism of the oligomeric streptolysin O pore: The early membrane lesion is lined by a free edge of the lipid membrane and is extended gradually during oligomerization
20. The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins
21. Crystal structure of the anthrax toxin protective antigen
22. Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form
23. The molecular mechanism of pneumolysin, a virulence factor from Streptococcus pneumoniae
24. The mechanism of membrane insertion for a cholesterol-dependent cytolysin: A novel paradigm for pore-forming toxins
25. Identification of a membrane-spanning domain of the thiol-activated pore-forming toxin Clostridium perfringens perfringolysin: An α-helical to β-sheet transition identified by fluorescence spectroscopy
26. Structure-based prediction of the conductance properties of ion channels
27. Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore