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[[Image:1eu4.jpg|left|200px]]<br /><applet load="1eu4" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1eu4, resolution 2.50&Aring;" />
'''CRYSTAL STRUCTURE OF THE SUPERANTIGEN SPE-H (ZINC BOUND) FROM STREPTOCOCCUS PYOGENES'''<br />


==Overview==
==CRYSTAL STRUCTURE OF THE SUPERANTIGEN SPE-H (ZINC BOUND) FROM STREPTOCOCCUS PYOGENES==
Bacterial superantigens (SAgs) are a structurally related group of protein toxins secreted by Staphylococcus aureus and Streptococcus pyogenes. They are implicated in a range of human pathologies associated with bacterial infection whose symptoms result from SAg-mediated stimulation of a large number (2-20%) of T-cells. At the molecular level, bacterial SAgs bind to major histocompatability class II (MHC-II) molecules and disrupt the normal interaction between MHC-II and T-cell receptors (TCRs). We have determined high-resolution crystal structures of two newly identified streptococcal superantigens, SPE-H and SMEZ-2. Both structures conform to the generic bacterial superantigen folding pattern, comprising an OB-fold N-terminal domain and a beta-grasp C-terminal domain. SPE-H and SMEZ-2 also display very similar zinc-binding sites on the outer concave surfaces of their C-terminal domains. Structural comparisons with other SAgs identify two structural sub-families. Sub-families are related by conserved core residues and demarcated by variable binding surfaces for MHC-II and TCR. SMEZ-2 is most closely related to the streptococcal SAg SPE-C, and together they constitute one structural sub-family. In contrast, SPE-H appears to be a hybrid whose N-terminal domain is most closely related to the SEB sub-family and whose C-terminal domain is most closely related to the SPE-C/SMEZ-2 sub-family. MHC-II binding for both SPE-H and SMEZ-2 is mediated by the zinc ion at their C-terminal face, whereas the generic N-terminal domain MHC-II binding site found on many SAgs appears not to be present. Structural comparisons provide evidence for variations in TCR binding between SPE-H, SMEZ-2 and other members of the SAg family; the extreme potency of SMEZ-2 (active at 10(-15) g ml-1 levels) is likely to be related to its TCR binding properties. The smez gene shows allelic variation that maps onto a considerable proportion of the protein surface. This allelic variation, coupled with the varied binding modes of SAgs to MHC-II and TCR, highlights the pressure on SAgs to avoid host immune defences.
<StructureSection load='1eu4' size='340' side='right'caption='[[1eu4]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1eu4]] 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=1EU4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EU4 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1eu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eu4 OCA], [https://pdbe.org/1eu4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eu4 RCSB], [https://www.ebi.ac.uk/pdbsum/1eu4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eu4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SPEH_STRPY SPEH_STRPY] Mitogenic for human peripheral blood lymphocytes.
== 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/eu/1eu4_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=1eu4 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1EU4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EU4 OCA].
*[[Exotoxin 3D structures|Exotoxin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Conservation and variation in superantigen structure and activity highlighted by the three-dimensional structures of two new superantigens from Streptococcus pyogenes., Arcus VL, Proft T, Sigrell JA, Baker HM, Fraser JD, Baker EN, J Mol Biol. 2000 May 26;299(1):157-68. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10860729 10860729]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Streptococcus pyogenes]]
[[Category: Streptococcus pyogenes]]
[[Category: Arcus, V L.]]
[[Category: Arcus VL]]
[[Category: Baker, E N.]]
[[Category: Baker EN]]
[[Category: Baker, H M.]]
[[Category: Baker HM]]
[[Category: Fraser, J D.]]
[[Category: Fraser JD]]
[[Category: Proft, T.]]
[[Category: Proft T]]
[[Category: Sigrell, J A.]]
[[Category: Sigrell JA]]
[[Category: ZN]]
[[Category: beta grasp]]
[[Category: ob fold]]
[[Category: superantigen fold]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:31:30 2008''

Latest revision as of 13:06, 20 March 2024

CRYSTAL STRUCTURE OF THE SUPERANTIGEN SPE-H (ZINC BOUND) FROM STREPTOCOCCUS PYOGENESCRYSTAL STRUCTURE OF THE SUPERANTIGEN SPE-H (ZINC BOUND) FROM STREPTOCOCCUS PYOGENES

Structural highlights

1eu4 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 2.5Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SPEH_STRPY Mitogenic for human peripheral blood lymphocytes.

Evolutionary Conservation

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

See Also

1eu4, resolution 2.50Å

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