3lkf
From Proteopedia
(New page: 200px<br /><applet load="3lkf" size="450" color="white" frame="true" align="right" spinBox="true" caption="3lkf, resolution 1.90Å" /> '''LEUKOCIDIN F (HLGB) ...) |
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| - | [[Image:3lkf.jpg|left|200px]]<br /><applet load="3lkf" size=" | + | [[Image:3lkf.jpg|left|200px]]<br /><applet load="3lkf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="3lkf, resolution 1.90Å" /> | caption="3lkf, resolution 1.90Å" /> | ||
'''LEUKOCIDIN F (HLGB) FROM STAPHYLOCOCCUS AUREUS WITH PHOSPHOCHOLINE BOUND'''<br /> | '''LEUKOCIDIN F (HLGB) FROM STAPHYLOCOCCUS AUREUS WITH PHOSPHOCHOLINE BOUND'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Staphylococcal LukF, LukS, HgammaII, and alpha-hemolysin are | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 3LKF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with PC as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 3LKF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with <scene name='pdbligand=PC:'>PC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LKF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
| - | [[Category: Gouaux, J | + | [[Category: Gouaux, J E.]] |
[[Category: Kamio, Y.]] | [[Category: Kamio, Y.]] | ||
[[Category: Nariya, H.]] | [[Category: Nariya, H.]] | ||
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[[Category: pore-forming toxin]] | [[Category: pore-forming toxin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:10:04 2008'' |
Revision as of 17:10, 21 February 2008
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LEUKOCIDIN F (HLGB) FROM STAPHYLOCOCCUS AUREUS WITH PHOSPHOCHOLINE BOUND
Overview
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.
About this Structure
3LKF is a Single protein structure of sequence from Staphylococcus aureus with as ligand. Full crystallographic information is available from OCA.
Reference
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
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