1goz

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[[Image:1goz.gif|left|200px]]
 
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==Structural basis for the altered T-cell receptor binding specificty in a superantigenic staphylococcus aureus Enterotoxin-B mutant==
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The line below this paragraph, containing "STRUCTURE_1goz", creates the "Structure Box" on the page.
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<StructureSection load='1goz' size='340' side='right'caption='[[1goz]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1goz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GOZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GOZ FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2&#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=1goz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1goz OCA], [https://pdbe.org/1goz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1goz RCSB], [https://www.ebi.ac.uk/pdbsum/1goz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1goz ProSAT]</span></td></tr>
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{{STRUCTURE_1goz| PDB=1goz | SCENE= }}
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</table>
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== Function ==
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'''STRUCTURAL BASIS FOR THE ALTERED T-CELL RECEPTOR BINDING SPECIFICTY IN A SUPERANTIGENIC STAPHYLOCOCCUS AUREUS ENTEROTOXIN-B MUTANT'''
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[https://www.uniprot.org/uniprot/ETXB_STAAU ETXB_STAAU] Staphylococcal enterotoxins cause the intoxication staphylococcal food poisoning syndrome. The illness characterized by high fever, hypotension, diarrhea, shock, and in some cases death.
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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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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/go/1goz_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=1goz ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
Bacterial superantigens are potent T-cell stimulatory protein molecules produced by Staphylococcus aureus and Streptococcus pyogenes. Their superantigenic activity can be attributed to their ability to cross-link major histocompatibility complex class II molecules with T-cell receptors (TCRs) to form a tri-molecular complex. Each superantigen is known to interact with a specific V(beta) element of TCR. Staphylococcal enterotoxin B (SEB, a superantigen), a primary cause of food poisoning, is also responsible for a significant percentage of non-menstrual associated toxic shock syndrome in patients with a variety of staphylococcal infections. Structural studies have elucidated a binding cavity on the toxin molecule essential for TCR binding. To understand the crucial residues involved in binding, mutagenesis analysis was performed. Our analysis suggest that mutation of a conserved residue Thr(112) to Ser (T112S) in the binding cavity induces a selective reduction in the affinity for binding one TCR V(beta) family and can be attributed to the structural differences in the native and mutant toxins. We present a detailed comparison of the mutant structure determined at 2.0 A with the previously reported native SEB and SEB-TCR V(beta) complex structures.
Bacterial superantigens are potent T-cell stimulatory protein molecules produced by Staphylococcus aureus and Streptococcus pyogenes. Their superantigenic activity can be attributed to their ability to cross-link major histocompatibility complex class II molecules with T-cell receptors (TCRs) to form a tri-molecular complex. Each superantigen is known to interact with a specific V(beta) element of TCR. Staphylococcal enterotoxin B (SEB, a superantigen), a primary cause of food poisoning, is also responsible for a significant percentage of non-menstrual associated toxic shock syndrome in patients with a variety of staphylococcal infections. Structural studies have elucidated a binding cavity on the toxin molecule essential for TCR binding. To understand the crucial residues involved in binding, mutagenesis analysis was performed. Our analysis suggest that mutation of a conserved residue Thr(112) to Ser (T112S) in the binding cavity induces a selective reduction in the affinity for binding one TCR V(beta) family and can be attributed to the structural differences in the native and mutant toxins. We present a detailed comparison of the mutant structure determined at 2.0 A with the previously reported native SEB and SEB-TCR V(beta) complex structures.
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==About this Structure==
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Structural and functional role of threonine 112 in a superantigen Staphylococcus aureus enterotoxin B.,Baker MD, Papageorgiou AC, Titball RW, Miller J, White S, Lingard B, Lee JJ, Cavanagh D, Kehoe MA, Robinson JH, Acharya KR J Biol Chem. 2002 Jan 25;277(4):2756-62. Epub 2001 Nov 9. PMID:11704673<ref>PMID:11704673</ref>
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1GOZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GOZ OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structural and functional role of threonine 112 in a superantigen Staphylococcus aureus enterotoxin B., Baker MD, Papageorgiou AC, Titball RW, Miller J, White S, Lingard B, Lee JJ, Cavanagh D, Kehoe MA, Robinson JH, Acharya KR, J Biol Chem. 2002 Jan 25;277(4):2756-62. Epub 2001 Nov 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11704673 11704673]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 1goz" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
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[[Category: Acharya, K R.]]
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[[Category: Acharya KR]]
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[[Category: Baker, M D.]]
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[[Category: Baker MD]]
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[[Category: Papageorgiou, A C.]]
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[[Category: Papageorgiou AC]]
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[[Category: Enterotoxin b]]
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[[Category: Seb]]
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[[Category: Staphylococcal enterotoxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:50:21 2008''
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Current revision

Structural basis for the altered T-cell receptor binding specificty in a superantigenic staphylococcus aureus Enterotoxin-B mutant

PDB ID 1goz

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