Structural basis of activity and allosteric control of diguanylate cyclase.

@article{Chan2004StructuralBO,
  title={Structural basis of activity and allosteric control of diguanylate cyclase.},
  author={Carmen Chan and Ralf Paul and Dietrich Samoray and Nicolas Amiot and Bernd Giese and Urs Jenal and Tilman Schirmer},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2004},
  volume={101 49},
  pages={
          17084-9
        }
}
Recent discoveries suggest that a novel second messenger, bis-(3'-->5')-cyclic di-GMP (c-diGMP), is extensively used by bacteria to control multicellular behavior. Condensation of two GTP to the dinucleotide is catalyzed by the widely distributed diguanylate cyclase (DGC or GGDEF) domain that occurs in various combinations with sensory and/or regulatory modules. The crystal structure of the unorthodox response regulator PleD from Caulobacter crescentus, which consists of two CheY-like receiver… CONTINUE READING
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