PDB ID or protein name

1pfo » Perfringolysin

1pfo » Perfringolysin
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Topology in Secreted
Topologyout side
in side
1pfo » Perfringolysin
Depth 4.4 ± 2.0 Å
Tilt Angle 38 ± 12°
ΔGtransfer -6.7 kcal/mol
Links to 1pfo PDB Sum, PDB, SCOP, MSD, OCA, MMDB
Topology out
Resolution 2.2 Å
Other PDB entries representing this structure 1m3i, 1m3j, 2bk1, 2bk2, 5dhl
Number of subunits 1
Experimental Verification for 1pfo » Perfringolysin
W466 is embedded in the bilayer core, while W464 and W467 may be structurally important but do not interact strongly with membrane. This is consistent with studies of Sekino-Suzuki et al. (1996) and Nakamura et al. (1998). The elongated protein is approximately perpendicular to the membrane based on FRET data (Ramachandran et al. 2005).
3 references
Nakamura M, Sekino-Suzuki N, Mitsui K, Ohno-Iwashita Y. 1998. Contribution of tryptophan residues to the structural changes in perfringolysin O during interaction with liposomal membranes. J Biochem (Tokyo). 123: 1145-55. PubMed
Ramachandran R., Tweten, R.K., and Johnson, A.E. 2005. The domains of a cholesterol-dependent cytolysin undergo a major FRET-detected rearrangement during pore formation. Proc. Natl. Acad. Sci. U. S. A. 102:7139-7144. PubMed
Sekino-Suzuki N, Nakamura M, Mitsui KI, Ohno-Iwashita Y. 1996. Contribution of individual tryptophan residues to the structure and activity of theta-toxin (perfringolysin O), a cholesterol-binding cytolysin. Eur J Biochem. 241: 941-7. PubMed
Comments on 1pfo » Perfringolysin
Sulfhydryl-activated toxin. Binds cholesterol (residue 459). Undergoes major conformational transitions and oligomerization upon association with membranes. Forms oligomers in the host membrane.