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[[Image:1dt2.gif|left|200px]]<br /><applet load="1dt2" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1dt2, resolution 2.8&Aring;" />
'''CRYSTAL STRUCTURE OF EXFOLIATIVE TOXIN B'''<br />


==Overview==
==CRYSTAL STRUCTURE OF EXFOLIATIVE TOXIN B==
Staphylococcal aureus epidermolytic toxins (ETs) A and B are responsible for the induction of staphylococcal scalded skin syndrome, a disease of neonates and young children. The clinical features of this syndrome vary from localized blisters to severe exfoliation affecting most of the body surface. Comparison of the crystal structures of two subtypes of ETs-rETA (at 2.0 A resolution), rETB (at 2.8 A resolution), and an active site variant of rETA, Ser195Ala at 2.0 A resolution has demonstrated that their overall topology resembles that of a "trypsin-like" serine protease, but with significant differences at the N- and C-termini and loop regions. The details of the catalytic site in both ET structures are very similar to those in glutamate-specific serine proteases, suggesting a common catalytic mechanism. However, the "oxyanion hole," which is part of the catalytic sites of glutamate specific serine proteases, is in the closed or inactive conformation for rETA, yet in the open or active conformation for rETB. The ETs contain a unique amphipathic helix at the N-terminus, and it appears to be involved in optimizing the conformation of the catalytic site residues. Determination of the structure of the rETA catalytic site variant, Ser195Ala, showed no significant perturbation at the active site, establishing that the loss of biological and esterolytic activity can be attributed solely to disruption of the catalytic serine residue. Finally, the crystal structure of ETs, together with biochemical data and mutagenesis studies, strongly confirms the classification of these molecules as "serine proteases" rather than "superantigens."
<StructureSection load='1dt2' size='340' side='right'caption='[[1dt2]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1dt2]] is a 1 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=1DT2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DT2 FirstGlance]. <br>
1DT2 is a [http://en.wikipedia.org/wiki/Single_protein 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=1DT2 OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</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=1dt2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dt2 OCA], [https://pdbe.org/1dt2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dt2 RCSB], [https://www.ebi.ac.uk/pdbsum/1dt2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dt2 ProSAT]</span></td></tr>
==Reference==
</table>
Structural similarities and differences in Staphylococcus aureus exfoliative toxins A and B as revealed by their crystal structures., Papageorgiou AC, Plano LR, Collins CM, Acharya KR, Protein Sci. 2000 Mar;9(3):610-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10752623 10752623]
== Function ==
[[Category: Single protein]]
[https://www.uniprot.org/uniprot/ETB_STAAU ETB_STAAU] Has serine protease-like properties and binds to the skin protein profilaggrin. Cleaves substrates after acidic residues. Exfoliative toxins cause impetigous diseases commonly referred as staphylococcal scalded skin syndrome (SSSS).<ref>PMID:2117445</ref> <ref>PMID:2384148</ref>
== 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/dt/1dt2_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=1dt2 ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
[[Category: Acharya, K R.]]
[[Category: Acharya KR]]
[[Category: Collins, C M.]]
[[Category: Collins CM]]
[[Category: Papageorgiou, A C.]]
[[Category: Papageorgiou AC]]
[[Category: Plano, L R.W.]]
[[Category: Plano LRW]]
[[Category: epidermolysis]]
[[Category: serine protease]]
[[Category: superantigen]]
[[Category: toxin]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:20:14 2008''

Latest revision as of 09:58, 7 February 2024

CRYSTAL STRUCTURE OF EXFOLIATIVE TOXIN BCRYSTAL STRUCTURE OF EXFOLIATIVE TOXIN B

Structural highlights

1dt2 is a 1 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ETB_STAAU Has serine protease-like properties and binds to the skin protein profilaggrin. Cleaves substrates after acidic residues. Exfoliative toxins cause impetigous diseases commonly referred as staphylococcal scalded skin syndrome (SSSS).[1] [2]

Evolutionary Conservation

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

References

  1. Bailey CJ, Smith TP. The reactive serine residue of epidermolytic toxin A. Biochem J. 1990 Jul 15;269(2):535-7. PMID:2117445
  2. Dancer SJ, Garratt R, Saldanha J, Jhoti H, Evans R. The epidermolytic toxins are serine proteases. FEBS Lett. 1990 Jul 30;268(1):129-32. PMID:2384148

1dt2, resolution 2.80Å

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