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[[Image:2qk7.jpg|left|200px]]
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{{STRUCTURE_2qk7|  PDB=2qk7  |  SCENE=  }}
'''A covalent S-F heterodimer of staphylococcal gamma-hemolysin'''


==A covalent S-F heterodimer of staphylococcal gamma-hemolysin==
<StructureSection load='2qk7' size='340' side='right'caption='[[2qk7]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</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>
== 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qk/2qk7_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qk7 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:18214982</ref>
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 Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2QK7 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QK7 OCA].
</div>
<div class="pdbe-citations 2qk7" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/18214982 18214982]
*[[Hemolysin 3D structures|Hemolysin 3D structures]]
[[Category: Protein complex]]
== References ==
[[Category: Staphylococcus aureus]]
<references/>
[[Category: Guillet, V.]]
__TOC__
[[Category: Maveyraud, L.]]
</StructureSection>
[[Category: Mourey, L.]]
[[Category: Large Structures]]
[[Category: Roblin, P.]]
[[Category: Staphylococcus aureus subsp. aureus MW2]]
[[Category: Beta-barrel]]
[[Category: Guillet V]]
[[Category: Covalent complex]]
[[Category: Maveyraud L]]
[[Category: Cytolysis]]
[[Category: Mourey L]]
[[Category: Hemolysis]]
[[Category: Roblin P]]
[[Category: Molecular plasticity]]
[[Category: Pore-forming toxin]]
[[Category: Protein-protein interaction]]
[[Category: Secreted]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 15:06:17 2008''

Latest revision as of 08:33, 30 October 2024

A covalent S-F heterodimer of staphylococcal gamma-hemolysin

2qk7, resolution 2.40Å

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