Structural highlights
Function
[HLGB_STAAU] Toxin that seems to act by forming pores in the membrane of the cell. Has a hemolytic and a leucotoxic activity.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Staphylococcal LukF, LukS, HgammaII, and alpha-hemolysin are self-assembling, channel-forming proteins related in sequence and function. In the alpha-hemolysin heptamer, the channel-forming beta-strands and the amino latch make long excursions from the protomer core. Here we report the crystal structure of the water soluble form of LukF. In the LukF structure the channel-forming region folds into an amphipathic, three-strand beta-sheet and the amino latch forms a beta-strand extending a central beta-sheet. The LukF structure illustrates how a channel-forming toxin masks protein-protein and protein-membrane interfaces prior to cell binding and assembly, and together with the alpha-hemolysin heptamer structure, they define the end points on the pathway of toxin assembly.
Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel.,Olson R, Nariya H, Yokota K, Kamio Y, Gouaux E Nat Struct Biol. 1999 Feb;6(2):134-40. PMID:10048924[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Olson R, Nariya H, Yokota K, Kamio Y, Gouaux E. Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel. Nat Struct Biol. 1999 Feb;6(2):134-40. PMID:10048924 doi:10.1038/5821
