View source for 4d3g


==Structure of PstA==
<StructureSection load='4d3g' size='340' side='right'caption='[[4d3g]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4d3g]] 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=4D3G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D3G 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]] 3&#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=4d3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d3g OCA], [https://pdbe.org/4d3g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d3g RCSB], [https://www.ebi.ac.uk/pdbsum/4d3g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d3g ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q2G229_STAA8 Q2G229_STAA8] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Signaling nucleotides are integral parts of signal transduction systems allowing bacteria to cope with and rapidly respond to changes in the environment. The Staphylococcus aureus PII-like signal transduction protein PstA was recently identified as a cyclic diadenylate monophosphate (c-di-AMP) binding protein. Here, we present the crystal structures of the apo and c-di-AMP bound PstA protein, which is trimeric in solution as well as in the crystals. The structures combined with a detailed bioinformatics analysis revealed that the protein belongs to a new family of proteins with a similar core fold but with distinct features to classical PII proteins, which usually function in nitrogen metabolism pathways in bacteria. The complex structure revealed three identical c-di-AMP binding sites per trimer with each binding site at a monomer-monomer interface. While distinctly different from other cyclic-di-nucleotide binding sites, as the half binding sites are not symmetrical, the complex structure also highlighted common features for c-di-AMP binding sites. A comparison between the apo and complex structures reveal a series of conformational changes that result in the ordering of two anti-parallel beta-strands that protrude from each monomer and allowed us to propose a mechanism on how the PstA protein functions as a signaling transduction protein.

Complex Structure and Biochemical Characterization of the Staphylococcus aureus cyclic di-AMP binding Protein PstA, the Founding Member of a New Signal Transduction Protein Family.,Campeotto I, Zhang Y, Mladenov MG, Freemont PS, Grundling A J Biol Chem. 2014 Dec 11. pii: jbc.M114.621789. PMID:25505271<ref>PMID:25505271</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4d3g" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus]]
[[Category: Campeotto I]]
[[Category: Freemont P]]
[[Category: Grundling A]]