Crystal structure of staphylococcal lukF delineates conformational changes accompanying formation of a transmembrane channel

R. Olson, H. Nariya, K. Yokota, Y. Kamio, Eric Gouaux

Research output: Contribution to journalArticle

183 Citations (Scopus)

Abstract

Staphylococcal LukF, LukS, HγII, and α-hemolysin are self-assembling, channel-forming proteins related in sequence and function. In the α- hemolysin heptamer, the channel-forming β-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 β-sheet and the amino latch forms a β-strand extending a central β-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 α-hemolysin heptamer structure, they define the end points on the pathway of toxin assembly.

Original languageEnglish (US)
Pages (from-to)134-140
Number of pages7
JournalNature Structural Biology
Volume6
Issue number2
DOIs
StatePublished - 1999
Externally publishedYes

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Hemolysin Proteins
Crystal structure
Proteins
Protein Subunits
Masks
Membrane Proteins
Water

ASJC Scopus subject areas

  • Biochemistry
  • Structural Biology
  • Genetics

Cite this

Crystal structure of staphylococcal lukF delineates conformational changes accompanying formation of a transmembrane channel. / Olson, R.; Nariya, H.; Yokota, K.; Kamio, Y.; Gouaux, Eric.

In: Nature Structural Biology, Vol. 6, No. 2, 1999, p. 134-140.

Research output: Contribution to journalArticle

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