Imperial College London


Faculty of MedicineDepartment of Infectious Disease

Chair in Protein Crystallography



+44 (0)20 7594 5327p.freemont




259Sir Alexander Fleming BuildingSouth Kensington Campus






BibTex format

author = {Schuster, C and Bellows, L and Tosi, T and Campeotto and Corrigan and Freemont, P and Grundling, A},
doi = {10.1126/scisignal.aaf7279},
journal = {Science Signaling},
pages = {ra81--ra81},
title = {The second messenger c-di-AMP inhibits the osmolyte uptake system OpuC in Staphylococcus aureus},
url = {},
volume = {9},
year = {2016}

RIS format (EndNote, RefMan)

AB - 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 LACΔgdpP 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.
AU - Schuster,C
AU - Bellows,L
AU - Tosi,T
AU - Campeotto
AU - Corrigan
AU - Freemont,P
AU - Grundling,A
DO - 10.1126/scisignal.aaf7279
EP - 81
PY - 2016///
SN - 1945-0877
SP - 81
TI - The second messenger c-di-AMP inhibits the osmolyte uptake system OpuC in Staphylococcus aureus
T2 - Science Signaling
UR -
UR -;9/441/ra81?ijkey=SZluRyjzK/0hw&keytype=ref&siteid=sigtrans
UR -
VL - 9
ER -