2qk7: Difference between revisions
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<StructureSection load='2qk7' size='340' side='right'caption='[[2qk7]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='2qk7' size='340' side='right'caption='[[2qk7]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2qk7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2qk7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_MW2 Staphylococcus aureus subsp. aureus MW2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QK7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QK7 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qk7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qk7 OCA], [https://pdbe.org/2qk7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qk7 RCSB], [https://www.ebi.ac.uk/pdbsum/2qk7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qk7 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qk7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qk7 OCA], [https://pdbe.org/2qk7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qk7 RCSB], [https://www.ebi.ac.uk/pdbsum/2qk7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qk7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/HLGA_STAAU HLGA_STAAU] Toxin that seems to act by forming pores in the membrane of the cell. Has a hemolytic and a leucotoxic activity. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Staphylococcus aureus subsp. aureus MW2]] | ||
[[Category: Guillet | [[Category: Guillet V]] | ||
[[Category: Maveyraud | [[Category: Maveyraud L]] | ||
[[Category: Mourey | [[Category: Mourey L]] | ||
[[Category: Roblin | [[Category: Roblin P]] | ||
Revision as of 14:34, 30 August 2023
A covalent S-F heterodimer of staphylococcal gamma-hemolysinA covalent S-F heterodimer of staphylococcal gamma-hemolysin
Structural highlights
FunctionHLGA_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 PubMedStaphylococcal 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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