2qk7: Difference between revisions
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= hlgA, hlg2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus]), hlgB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus]) | |GENE= hlgA, hlg2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus]), hlgB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1lkf|1LKF]], [[2lkf|2LKF]], [[3lkf|3LKF]], [[1pvl|1PVL]], [[1t5r|1T5R]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qk7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qk7 OCA], [http://www.ebi.ac.uk/pdbsum/2qk7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qk7 RCSB]</span> | |||
}} | }} | ||
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[[Category: secreted]] | [[Category: secreted]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:50:13 2008'' | ||
Revision as of 04:50, 31 March 2008
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| , resolution 2.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | hlgA, hlg2 (Staphylococcus aureus), hlgB (Staphylococcus aureus) | ||||||
| Related: | 1LKF, 2LKF, 3LKF, 1PVL, 1T5R
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
A covalent S-F heterodimer of staphylococcal gamma-hemolysin
OverviewOverview
Staphylococcal leucotoxins, leucocidins, and gamma-hemolysins are bicomponent beta-barrel pore-forming toxins (beta-PFTs). Their production is associated with several clinical diseases. They have cytotoxic activity due to the synergistic action of a class S component and a class F component, which are secreted as water-soluble monomers and form hetero-oligomeric transmembrane pores, causing the lysis of susceptible cells. Structural information is currently available for the monomeric S and F proteins and the homoheptamer formed by the related alpha-hemolysin. These structures illustrate the start and end points in the mechanistic framework of beta-PFT assembly. Only limited structural data exist for the intermediate stages, including hetero-oligomeric complexes of leucotoxins. We investigated the protein-protein interactions responsible for maintaining the final bipartite molecular architecture and describe here the high-resolution crystal structure and low-resolution solution structure of a site-specific cross-linked heterodimer of gamma-hemolysin (HlgA T28C-HlgB N156C), which were solved by X-ray crystallography and small angle X-ray scattering, respectively. These structures reveal a molecular plasticity of beta-PFTs, which may facilitate the transition from membrane-bound monomers to heterodimers. Proteins 2008. (c) 2008 Wiley-Liss, Inc.
About this StructureAbout this Structure
2QK7 is a Protein complex structure of sequences from Staphylococcus aureus. Full crystallographic information is available from OCA.
ReferenceReference
A covalent S-F heterodimer of leucotoxin reveals molecular plasticity of beta-barrel pore-forming toxins., Roblin P, Guillet V, Joubert O, Keller D, Erard M, Maveyraud L, Prevost G, Mourey L, Proteins. 2008 Jan 23;71(1):485-496. PMID:18214982
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