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1et6

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[[Image:1et6.jpg|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF THE SUPERANTIGEN SMEZ-2 FROM STREPTOCOCCUS PYOGENES==
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|PDB= 1et6 |SIZE=350|CAPTION= <scene name='initialview01'>1et6</scene>, resolution 1.90&Aring;
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<StructureSection load='1et6' size='340' side='right'caption='[[1et6]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1et6]] 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=1ET6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ET6 FirstGlance]. <br>
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|ACTIVITY=
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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]] 1.9&#8491;</td></tr>
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|GENE=
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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=1et6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1et6 OCA], [https://pdbe.org/1et6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1et6 RCSB], [https://www.ebi.ac.uk/pdbsum/1et6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1et6 ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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'''CRYSTAL STRUCTURE OF THE SUPERANTIGEN SMEZ-2 FROM STREPTOCOCCUS PYOGENES'''
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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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==Overview==
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Check<jmol>
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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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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/et/1et6_consurf.spt"</scriptWhenChecked>
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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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1ET6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ET6 OCA].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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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=1et6 ConSurf].
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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://www.ncbi.nlm.nih.gov/pubmed/10860729 10860729]
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<div style="clear:both"></div>
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[[Category: Single protein]]
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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: beta grasp]]
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[[Category: ob fold]]
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[[Category: superantigen fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:00:06 2008''
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Current revision

CRYSTAL STRUCTURE OF THE SUPERANTIGEN SMEZ-2 FROM STREPTOCOCCUS PYOGENES

PDB ID 1et6

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