1eu3

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(New page: 200px<br /><applet load="1eu3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eu3, resolution 1.68&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1eu3.jpg|left|200px]]<br /><applet load="1eu3" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1eu3, resolution 1.68&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE SUPERANTIGEN SMEZ-2 (ZINC BOUND) FROM STREPTOCOCCUS PYOGENES'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE SUPERANTIGEN SMEZ-2 (ZINC BOUND) FROM STREPTOCOCCUS PYOGENES==
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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.
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<StructureSection load='1eu3' size='340' side='right'caption='[[1eu3]], [[Resolution|resolution]] 1.68&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1eu3]] is a 2 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=1EU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EU3 FirstGlance]. <br>
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1EU3 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 PO4, ZN and K as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EU3 OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.68&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eu3 OCA], [https://pdbe.org/1eu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eu3 RCSB], [https://www.ebi.ac.uk/pdbsum/1eu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eu3 ProSAT]</span></td></tr>
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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]
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</table>
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[[Category: Single protein]]
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== Function ==
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[https://www.uniprot.org/uniprot/Q9RQQ5_STRPY Q9RQQ5_STRPY]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eu/1eu3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1eu3 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Streptococcus pyogenes]]
[[Category: Streptococcus pyogenes]]
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[[Category: Arcus, V.L.]]
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[[Category: Arcus VL]]
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[[Category: Baker, E.N.]]
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[[Category: Baker EN]]
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[[Category: Baker, H.M.]]
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[[Category: Baker HM]]
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[[Category: Fraser, J.D.]]
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[[Category: Fraser JD]]
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[[Category: Proft, T.]]
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[[Category: Proft T]]
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[[Category: Sigrell, J.A.]]
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[[Category: Sigrell JA]]
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[[Category: K]]
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[[Category: PO4]]
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[[Category: ZN]]
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[[Category: beta grasp]]
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[[Category: ob fold]]
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[[Category: superantigen fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:48:55 2007''
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Current revision

CRYSTAL STRUCTURE OF THE SUPERANTIGEN SMEZ-2 (ZINC BOUND) FROM STREPTOCOCCUS PYOGENES

PDB ID 1eu3

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