1ty0

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(New page: 200px<br /><applet load="1ty0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ty0, resolution 1.75&Aring;" /> '''Crystal structure of...)
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[[Image:1ty0.gif|left|200px]]<br /><applet load="1ty0" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ty0, resolution 1.75&Aring;" />
 
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'''Crystal structure of the streptococcal pyrogenic exotoxin J (SPE-J)'''<br />
 
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==Overview==
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==Crystal structure of the streptococcal pyrogenic exotoxin J (SPE-J)==
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The protein toxins known as superantigens (SAgs), which are expressed, primarily by the pathogenic bacteria Staphylococcus aureus and, Streptococcus pyogenes, are highly potent immunotoxins with the ability to, cause serious human disease. These SAgs share a conserved fold but quite, varied activities. In addition to their common role of cross-linking, T-cell receptors (TCRs) and major histocompatibility complex class II, (MHC-II) molecules, some SAgs can cross-link MHC-II, using diverse, mechanisms. The crystal structure of the streptococcal superantigen, streptococcal pyrogenic exotoxin J (SPE-J) has been solved at 1.75 A, resolution (R = 0.209, R(free) = 0.240), both with and without bound, Zn(2+). The structure displays the canonical two-domain SAg fold and a, zinc-binding site that is shared by a subset of other SAgs. Most, importantly, in concentrated solution and in the crystal, SPE-J forms, dimers. These dimers, which are present in two different crystal, environments, form via the same face that is used for TCR binding in other, SAgs. Site-directed mutagenesis shows that this face is also used for TCR, binding SPE-J. We infer that SPE-J cross-links TCR and MHC-II as a monomer, but that dimers may form on the antigen-presenting cell surface, cross-linking MHC-II and eliciting intracellular signaling.
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<StructureSection load='1ty0' size='340' side='right'caption='[[1ty0]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ty0]] is a 3 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=1TY0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TY0 FirstGlance]. <br>
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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]] 1.75&#8491;</td></tr>
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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=1ty0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ty0 OCA], [https://pdbe.org/1ty0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ty0 RCSB], [https://www.ebi.ac.uk/pdbsum/1ty0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ty0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q7BAE3_STRPY Q7BAE3_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/ty/1ty0_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=1ty0 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1TY0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TY0 OCA].
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*[[Exotoxin 3D structures|Exotoxin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystallographic and mutational data show that the streptococcal pyrogenic exotoxin J can use a common binding surface for T-cell receptor binding and dimerization., Baker HM, Proft T, Webb PD, Arcus VL, Fraser JD, Baker EN, J Biol Chem. 2004 Sep 10;279(37):38571-6. Epub 2004 Jul 7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15247241 15247241]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[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: Webb, P.D.]]
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[[Category: Webb PD]]
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[[Category: crystal structure]]
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[[Category: dimerization]]
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[[Category: mutagenesis]]
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[[Category: superantigen]]
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[[Category: t-cell receptor binding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:57:17 2007''
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Current revision

Crystal structure of the streptococcal pyrogenic exotoxin J (SPE-J)

PDB ID 1ty0

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