Origin of asymmetry in adenylyl cyclases: structures of Mycobacterium tuberculosis Rv1900c.

@article{Sinha2005OriginOA,
  title={Origin of asymmetry in adenylyl cyclases: structures of Mycobacterium tuberculosis Rv1900c.},
  author={Sangita C Sinha and Martina Wetterer and Stephen R Sprang and Joachim E Schultz and J{\"u}rgen Ulrich Linder},
  journal={The EMBO journal},
  year={2005},
  volume={24 4},
  pages={
          663-73
        }
}
Rv1900c, a Mycobacterium tuberculosis adenylyl cyclase, is composed of an N-terminal alpha/beta-hydrolase domain and a C-terminal cyclase homology domain. It has an unusual 7% guanylyl cyclase side-activity. A canonical substrate-defining lysine and a catalytic asparagine indispensable for mammalian adenylyl cyclase activity correspond to N342 and H402 in Rv1900c. Mutagenic analysis indicates that these residues are dispensable for activity of Rv1900c. Structures of the cyclase homology domain… CONTINUE READING
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