4ae5: Difference between revisions

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'''Unreleased structure'''


The entry 4ae5 is ON HOLD
==STRUCTURE OF A MAJOR REGULATOR OF STAPHYLOCOCCAL PATHOGENESIS==
<StructureSection load='4ae5' size='340' side='right'caption='[[4ae5]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<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 id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
<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>
<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;">
== Publication Abstract from PubMed ==
The 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.


Authors: HIRSHBERG, M.
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<ref>PMID:22750855</ref>


Description:
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ae5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus]]
[[Category: Henrick K]]
[[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

4ae5 is a 4 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 1.85Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2]

Publication Abstract from PubMed

The 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

  1. ↑ Balaban N, Goldkorn T, Gov Y, Hirshberg M, Koyfman N, Matthews HR, Nhan RT, Singh B, Uziel O. Regulation of Staphylococcus aureus pathogenesis via target of RNAIII-activating Protein (TRAP). J Biol Chem. 2001 Jan 26;276(4):2658-67. PMID:11160124 doi:10.1074/jbc.m005446200
  2. ↑ Korem M, Gov Y, Kiran MD, Balaban N. Transcriptional profiling of target of RNAIII-activating protein, a master regulator of staphylococcal virulence. Infect Immun. 2005 Oct;73(10):6220-8. PMID:16177293 doi:10.1128/IAI.73.10.6220-6228.2005
  3. ↑ Henrick K, Hirshberg M. Structure of the signal transduction protein TRAP (target of RNAIII-activating protein). Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jul 1;68(Pt 7):744-50., Epub 2012 Jun 22. PMID:22750855 doi:10.1107/S1744309112020167

4ae5, resolution 1.85Å

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