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Mycobacterium Tuberculosis
MTB DosS sensor controlled through heme binding of molecular oxygen or nitric oxide
January 17th, 2006
The Mycobacterium tuberculosis DosS sensor is controlled through heme binding of molecular oxygen or nitric oxide. According to recent research from England, "The majority of the Mycobacterium tuberculosis response to hypoxia and nitric oxide is through the DosRS (DevRS) two-component regulatory system. The N-terminal input domain of the DosS sensor contains two GAF domains." "We demonstrate here that the proximal GAF domain binds heme, and identified histidine 149 of DosS as critical to heme-binding; the location of this histidine residue is similar to the cGMP-binding site in. a crystal structure of cyclic nucleotide phosphodiesterase...
Source: TB & Outbreaks Week (2006-01-17)
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