3LKF
LEUKOCIDIN F (HLGB) FROM STAPHYLOCOCCUS AUREUS WITH PHOSPHOCHOLINE BOUND
Summary for 3LKF
| Entry DOI | 10.2210/pdb3lkf/pdb |
| Descriptor | LEUKOCIDIN F SUBUNIT, PHOSPHOCHOLINE (3 entities in total) |
| Functional Keywords | leukotoxin, hemolysin, pore-forming toxin, toxin |
| Biological source | Staphylococcus aureus |
| Total number of polymer chains | 1 |
| Total formula weight | 34274.87 |
| Authors | Olson, R.,Nariya, H.,Yokota, K.,Kamio, Y.,Gouaux, J.E. (deposition date: 1998-07-28, release date: 1999-07-28, Last modification date: 2024-04-03) |
| Primary citation | 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., 6:134-140, 1999 Cited by PubMed Abstract: 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. PubMed: 10048924DOI: 10.1038/5821 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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