1agj: Difference between revisions

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<StructureSection load='1agj' size='340' side='right'caption='[[1agj]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='1agj' size='340' side='right'caption='[[1agj]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1agj]] is a 2 chain structure with 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=1AGJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AGJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[1agj]] 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=1AGJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AGJ FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1agj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1agj OCA], [http://pdbe.org/1agj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1agj RCSB], [http://www.ebi.ac.uk/pdbsum/1agj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1agj ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#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=1agj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1agj OCA], [https://pdbe.org/1agj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1agj RCSB], [https://www.ebi.ac.uk/pdbsum/1agj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1agj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ETA_STAAU ETA_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>
[https://www.uniprot.org/uniprot/ETA_STAAU ETA_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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1agj ConSurf].
</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=1agj ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BACKGROUND: Staphylococcal epidermolytic toxins A and B (ETA and ETB) are responsible for the staphylococcal scalded skin syndrome of newborn and young infants; this condition can appear just a few hours after birth. These toxins cause the disorganization and disruption of the region between the stratum spinosum and the stratum granulosum--two of the three cellular layers constituting the epidermis. The physiological substrate of ETA is not known and, consequently, its mode of action in vivo remains an unanswered question. Determination of the structure of ETA and its comparison with other serine proteases may reveal insights into ETA's catalytic mechanism. RESULTS: The crystal structure of staphylococcal ETA has been determined by multiple isomorphous replacement and refined at 1.7 A resolution with a crystallographic R factor of 0.184. The structure of ETA reveals it to be a new and unique member of the trypsin-like serine protease family. In contrast to other serine protease folds, ETA can be characterized by ETA-specific surface loops, a lack of cysteine bridges, an oxyanion hole which is not preformed, an S1 specific pocket designed for a negatively charged amino acid and an ETA-specific specific N-terminal helix which is shown to be crucial for substrate hydrolysis. CONCLUSIONS: Despite very low sequence homology between ETA and other trypsin-like serine proteases, the ETA crystal structure, together with biochemical data and site-directed mutagenesis studies, strongly confirms the classification of ETA in the Glu-endopeptidase family. Direct links can be made between the protease architecture of ETA and its biological activity.
The structure of Staphylococcus aureus epidermolytic toxin A, an atypic serine protease, at 1.7 A resolution.,Cavarelli J, Prevost G, Bourguet W, Moulinier L, Chevrier B, Delagoutte B, Bilwes A, Mourey L, Rifai S, Piemont Y, Moras D Structure. 1997 Jun 15;5(6):813-24. PMID:9261066<ref>PMID:9261066</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1agj" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
[[Category: Cavarelli, J]]
[[Category: Cavarelli J]]
[[Category: Hydrolase]]
[[Category: Serine protease]]

Latest revision as of 09:30, 7 February 2024

EPIDERMOLYTIC TOXIN A FROM STAPHYLOCOCCUS AUREUSEPIDERMOLYTIC TOXIN A FROM STAPHYLOCOCCUS AUREUS

Structural highlights

1agj is a 2 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 1.7Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ETA_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

1agj, resolution 1.70Å

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