5iip

Staphylococcus aureus OpuCA

spinqualitylabelsall models 5iip, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5iip 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 2.5Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A160MQL0_STAAU 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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