4ae5: Difference between revisions
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==STRUCTURE OF A MAJOR REGULATOR OF STAPHYLOCOCCAL PATHOGENESIS== | ==STRUCTURE OF A MAJOR REGULATOR OF STAPHYLOCOCCAL PATHOGENESIS== | ||
<StructureSection load='4ae5' size='340' side='right' caption='[[4ae5]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='4ae5' size='340' side='right'caption='[[4ae5]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ae5]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ae5]] is a 4 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=4AE5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AE5 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>< | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr> | ||
<table> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ae5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ae5 OCA], [https://pdbe.org/4ae5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ae5 RCSB], [https://www.ebi.ac.uk/pdbsum/4ae5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ae5 ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TRAP_STAA8 TRAP_STAA8] Signal transduction protein, which is a major regulator of staphylococcal pathogenesis. Phosphorylated TRAP leads to the activation of agr system and consequent RNAIII synthesis resulting in the expression of several virulence factors. Up-regulates the expression of most toxins and genes known to be necessary for biofilm formation.<ref>PMID:11160124</ref> <ref>PMID:16177293</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4ae5" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
[[Category: Henrick | [[Category: Henrick K]] | ||
[[Category: Hirshberg | [[Category: Hirshberg M]] | ||
Latest revision as of 13:50, 9 May 2024
STRUCTURE OF A MAJOR REGULATOR OF STAPHYLOCOCCAL PATHOGENESISSTRUCTURE OF A MAJOR REGULATOR OF STAPHYLOCOCCAL PATHOGENESIS
Structural highlights
FunctionTRAP_STAA8 Signal transduction protein, which is a major regulator of staphylococcal pathogenesis. Phosphorylated TRAP leads to the activation of agr system and consequent RNAIII synthesis resulting in the expression of several virulence factors. Up-regulates the expression of most toxins and genes known to be necessary for biofilm formation.[1] [2] Publication Abstract from PubMedThe crystal structure of the signal transduction protein TRAP is reported at 1.85 A resolution. The structure of TRAP consists of a central eight-stranded beta-barrel flanked asymmetrically by helices and is monomeric both in solution and in the crystal structure. A formate ion was found bound to TRAP identically in all four molecules in the asymmetric unit. Structure of the signal transduction protein TRAP (target of RNAIII-activating protein).,Henrick K, Hirshberg M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jul 1;68(Pt 7):744-50., Epub 2012 Jun 22. PMID:22750855[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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