Adenylyl cyclase
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Adenylate cyclase is an enzyme with systematic name ATP diphosphate-lyase . It catalyzes the following reaction:ATP = 3′,5′-cyclic AMP + diphosphate
Adenylate cyclase (calmodulin sensitive) trimer, Bacillus anthracis Epinephrine binds its receptor, that associates with a heterotrimeric G protein. The G protein associates with adenylyl cyclase, which converts ATP to cAMP, spreading the signal.
Beta adrenergic receptor kinase pathway
Bacillus anthracis
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Bacillus anthracis is a gram-positive and rod-shaped bacterium that causes anthrax, a deadly disease to livestock and, occasionally, to humans. It is the only permanent (obligate) pathogen within the genus Bacillus. Its infection is a type of zoonosis, as it is transmitted from animals to humans. It was discovered by a German physician Robert Koch in 1876, and became the first bacterium to be experimentally shown as a pathogen. The discovery was also the first scientific evidence for the germ theory of diseases.
CD14 and Mac-1 work together to increase the macrophage internalization of B. anthracis spores. (a) CD14 and TLR2 work in close proximity to propagate the activation signal. Mac-1 starts in a closed confirmation which keeps the integrin from binding the spores, keeping them out of the cell. (b) CD14 binds the rhamnose residues on the BclA of the exosporium leading to TLR2-mediated activation of PI3K. (c) Activation of PI3K pushes Mac-1 into its open conformation so the spore can be bound and internalized (information from Oliva
CapD protein crystal structure of B. anthracis