View source for 5iip


==Staphylococcus aureus OpuCA==
<StructureSection load='5iip' size='340' side='right'caption='[[5iip]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5iip]] 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=5IIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IIP 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]] 2.5&#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=5iip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iip OCA], [https://pdbe.org/5iip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5iip RCSB], [https://www.ebi.ac.uk/pdbsum/5iip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5iip ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A160MQL0_STAAU A0A160MQL0_STAAU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Staphylococcus aureus is an important opportunistic human pathogen that is highly resistant to osmotic stresses. To survive an increase in osmolarity, bacteria immediately take up potassium ions and small organic compounds known as compatible solutes. The second messenger cyclic diadenosine monophosphate (c-di-AMP) reduces the ability of bacteria to withstand osmotic stress by binding to and inhibiting several proteins that promote potassium uptake. We identified OpuCA, the adenosine triphosphatase (ATPase) component of an uptake system for the compatible solute carnitine, as a c-di-AMP target protein in S aureus and found that the LAC*DeltagdpP strain of S aureus, which overproduces c-di-AMP, showed reduced carnitine uptake. The paired cystathionine-beta-synthase (CBS) domains of OpuCA bound to c-di-AMP, and a crystal structure revealed a putative binding pocket for c-di-AMP in the cleft between the two CBS domains. Thus, c-di-AMP inhibits osmoprotection through multiple mechanisms.

The second messenger c-di-AMP inhibits the osmolyte uptake system OpuC in Staphylococcus aureus.,Schuster CF, Bellows LE, Tosi T, Campeotto I, Corrigan RM, Freemont P, Grundling A Sci Signal. 2016 Aug 16;9(441):ra81. doi: 10.1126/scisignal.aaf7279. PMID:27531650<ref>PMID:27531650</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5iip" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus]]
[[Category: Campeotto I]]
[[Category: Freemont PS]]
[[Category: Grundling A]]
[[Category: Tosi T]]