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1agj

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Revision as of 14:53, 10 May 2019

EPIDERMOLYTIC 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.
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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bailey CJ, Smith TP. The reactive serine residue of epidermolytic toxin A. Biochem J. 1990 Jul 15;269(2):535-7. PMID:2117445
↑ 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
↑ Cavarelli J, Prevost G, Bourguet W, Moulinier L, Chevrier B, Delagoutte B, Bilwes A, Mourey L, Rifai S, Piemont Y, Moras D. The structure of Staphylococcus aureus epidermolytic toxin A, an atypic serine protease, at 1.7 A resolution. Structure. 1997 Jun 15;5(6):813-24. PMID:9261066

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1agj"

Categories: Large Structures | Staphylococcus aureus | Cavarelli, J | Hydrolase | Serine protease

@@ Line 1: / Line 1: @@
 ==EPIDERMOLYTIC TOXIN A FROM STAPHYLOCOCCUS AUREUS==
-<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 ==
 <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>
@@ Line 12: / Line 12: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ag/1agj_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ag/1agj_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 31: / Line 31: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Staphylococcus aureus]]
 [[Category: Cavarelli, J]]
 [[Category: Hydrolase]]
 [[Category: Serine protease]]

1agj

From Proteopedia

Revision as of 14:53, 10 May 2019

EPIDERMOLYTIC TOXIN A FROM STAPHYLOCOCCUS AUREUS

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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