5IIP
Staphylococcus aureus OpuCA
Summary for 5IIP
| Entry DOI | 10.2210/pdb5iip/pdb |
| Descriptor | Glycine betaine/carnitine/choline ABC transporter%2C ATP-binding protein%2C putative (2 entities in total) |
| Functional Keywords | cbs domain, osmoprotection, c-di-amp, transport protein |
| Biological source | Staphylococcus aureus |
| Total number of polymer chains | 4 |
| Total formula weight | 87489.58 |
| Authors | Tosi, T.,Campeotto, I.,Freemont, P.S.,Grundling, A. (deposition date: 2016-03-01, release date: 2016-08-24, Last modification date: 2024-01-10) |
| Primary citation | Schulte, L.E.,Schuster, C.F.,Tosi, T.,Campeotto, I.,Corrigan, R.M.,Freemont, P.S.,Grundling, A. The second messenger c-di-AMP inhibits the osmolyte uptake system OpuC in Staphylococcus aureus. Sci.Signal., 9:441-, 2016 Cited by PubMed Abstract: 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*ΔgdpP strain of S aureus, which overproduces c-di-AMP, showed reduced carnitine uptake. The paired cystathionine-β-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. PubMed: 27531650DOI: 10.1126/scisignal.aaf7279 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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