We determined the crystal structure of the full-length cAMP phosphodiesterase Rv0805 from Mycobacterium tuberculosis. Furthermore we showed, that localization of Rv0805 to the bacterial cell wall is dependent on its C terminus, and expression of either wild type or mutationally inactivated Rv0805 in M. smegmatis alters cell permeability to hydrophobic cytotoxic compounds. Rv0805 may therefore play a key role in the pathogenicity of mycobacteria, not only by hydrolyzing bacterial cAMP, but also by moonlighting as a protein that can alter cell wall functioning.
COBISS.SI-ID: 4259610
At the meeting of Slovenian Biochemical Society with the international participation, we were invited to orally present our recent results (lecture by M. Podobnik), paper from the Chapter 6.1. Thus, we presented our results on the structural and functional studies on cAMP-mediated cell signaling in mycobacteria, and especially on the unique cAMP phosphodiesterase Rv0805 from Mycobacaterium tuberculosis, which has been a major topic of our studies for the past years.
COBISS.SI-ID: 4259866