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[[Image:1an8.gif|left|200px]]<br />
<applet load="1an8" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1an8, resolution 2.4&Aring;" />
'''CRYSTAL STRUCTURE OF THE STREPTOCOCCAL SUPERANTIGEN SPE-C'''<br />


==Overview==
==CRYSTAL STRUCTURE OF THE STREPTOCOCCAL SUPERANTIGEN SPE-C==
Bacterial superantigens are small proteins that have a very potent, stimulatory effect on T lymphocytes through their ability to bind to both, MHC class II molecules and T-cell receptors. We have determined the, three-dimensional structure of a Streptococcal superantigen, SPE-C, at 2.4, A resolution. The structure shows that SPE-C has the usual superantigen, fold, but that the surface that forms a generic, low-affinity MHC-binding, site in other superantigens is here used to create a SPE-C dimer. Instead, MHC class II binding occurs through a zinc binding site that is analogous, to a similar site in staphylococcal enterotoxin A. Consideration of the, SPE-C dimer suggests a novel mechanism for promotion of MHC aggregation, and T-cell activation.
<StructureSection load='1an8' size='340' side='right'caption='[[1an8]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1an8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AN8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AN8 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=1an8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1an8 OCA], [https://pdbe.org/1an8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1an8 RCSB], [https://www.ebi.ac.uk/pdbsum/1an8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1an8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SPEC_STRP8 SPEC_STRP8] Superantigen that acts as a causative agent of the symptoms associated with scarlet fever (PubMed:1500157, PubMed:1987034, PubMed:9253413, PubMed:11163233). Has been associated with streptococcal toxic shock-like disease and may play a role in the early events of rheumatic fever (PubMed:1500157, PubMed:9253413, PubMed:11163233). Superantigens cross-link major histocompatibility complex (MHC) class II and T-cell receptor (TCR) molecules, resulting in an overstimulation of T-cells associated with a massive release of pyrogenic and inflammatory cytokines (PubMed:9253413, PubMed:11163233).<ref>PMID:11163233</ref> <ref>PMID:1500157</ref> <ref>PMID:1987034</ref> <ref>PMID:9253413</ref>
== 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/an/1an8_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1an8 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1AN8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Structure known Active Sites: ZNA and ZNB. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AN8 OCA].
*[[Exotoxin 3D structures|Exotoxin 3D structures]]
 
== References ==
==Reference==
<references/>
Crystal structure of the streptococcal superantigen SPE-C: dimerization and zinc binding suggest a novel mode of interaction with MHC class II molecules., Roussel A, Anderson BF, Baker HM, Fraser JD, Baker EN, Nat Struct Biol. 1997 Aug;4(8):635-43. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9253413 9253413]
__TOC__
[[Category: Single protein]]
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus pyogenes]]
[[Category: Streptococcus pyogenes]]
[[Category: Baker, E.N.]]
[[Category: Baker EN]]
[[Category: Roussel, A.]]
[[Category: Roussel A]]
[[Category: bacterial superantigen]]
[[Category: toxin]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 12:53:33 2007''

Latest revision as of 09:32, 7 February 2024

CRYSTAL STRUCTURE OF THE STREPTOCOCCAL SUPERANTIGEN SPE-CCRYSTAL STRUCTURE OF THE STREPTOCOCCAL SUPERANTIGEN SPE-C

Structural highlights

1an8 is a 1 chain structure with sequence from Streptococcus pyogenes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SPEC_STRP8 Superantigen that acts as a causative agent of the symptoms associated with scarlet fever (PubMed:1500157, PubMed:1987034, PubMed:9253413, PubMed:11163233). Has been associated with streptococcal toxic shock-like disease and may play a role in the early events of rheumatic fever (PubMed:1500157, PubMed:9253413, PubMed:11163233). Superantigens cross-link major histocompatibility complex (MHC) class II and T-cell receptor (TCR) molecules, resulting in an overstimulation of T-cells associated with a massive release of pyrogenic and inflammatory cytokines (PubMed:9253413, PubMed:11163233).[1] [2] [3] [4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Li Y, Li H, Dimasi N, McCormick JK, Martin R, Schuck P, Schlievert PM, Mariuzza RA. Crystal structure of a superantigen bound to the high-affinity, zinc-dependent site on MHC class II. Immunity. 2001 Jan;14(1):93-104. PMID:11163233
  2. ↑ Kapur V, Nelson K, Schlievert PM, Selander RK, Musser JM. Molecular population genetic evidence of horizontal spread of two alleles of the pyrogenic exotoxin C gene (speC) among pathogenic clones of Streptococcus pyogenes. Infect Immun. 1992 Sep;60(9):3513-7. PMID:1500157 doi:10.1128/iai.60.9.3513-3517.1992
  3. ↑ Yu CE, Ferretti JJ. Frequency of the erythrogenic toxin B and C genes (speB and speC) among clinical isolates of group A streptococci. Infect Immun. 1991 Jan;59(1):211-5. PMID:1987034 doi:10.1128/iai.59.1.211-215.1991
  4. ↑ Roussel A, Anderson BF, Baker HM, Fraser JD, Baker EN. Crystal structure of the streptococcal superantigen SPE-C: dimerization and zinc binding suggest a novel mode of interaction with MHC class II molecules. Nat Struct Biol. 1997 Aug;4(8):635-43. PMID:9253413

1an8, resolution 2.40Å

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