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<StructureSection load='1an8' size='340' side='right'caption='[[1an8]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='1an8' size='340' side='right'caption='[[1an8]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1an8]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AN8 FirstGlance]. <br>
<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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1an8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1an8 OCA], [http://pdbe.org/1an8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1an8 RCSB], [http://www.ebi.ac.uk/pdbsum/1an8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1an8 ProSAT]</span></td></tr>
</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>
</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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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].
</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>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:9253413<ref>PMID:9253413</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1an8" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Exotoxin|Exotoxin]]
*[[Exotoxin 3D structures|Exotoxin 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Baker, E N]]
[[Category: Streptococcus pyogenes]]
[[Category: Roussel, A]]
[[Category: Baker EN]]
[[Category: Bacterial superantigen]]
[[Category: Roussel A]]
[[Category: Toxin]]

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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