Crystal Structure of Human Soluble Adenylate Cyclase Reveals a Distinct, Highly Flexible Allosteric Bicarbonate Binding Pocket

@inproceedings{SaalauBethell2014CrystalSO,
  title={Crystal Structure of Human Soluble Adenylate Cyclase Reveals a Distinct, Highly Flexible Allosteric Bicarbonate Binding Pocket},
  author={Susanne M. Saalau-Bethell and Valerio Berdini and Anne Cleasby and Miles Congreve and Joseph E. Coyle and Victoria Lock and Christopher W. Murray and Michael A. O'Brien and Sharna J. Rich and Tracey Sambrook and Mladen Vinkovi{\'c} and Jeff R Yon and Harren Jhoti},
  booktitle={ChemMedChem},
  year={2014}
}
Soluble adenylate cyclases catalyse the synthesis of the second messenger cAMP through the cyclisation of ATP and are the only known enzymes to be directly activated by bicarbonate. Here, we report the first crystal structure of the human enzyme that reveals a pseudosymmetrical arrangement of two catalytic domains to produce a single competent active site and a novel discrete bicarbonate binding pocket. Crystal structures of the apo protein, the protein in complex with α,β-methylene adenosine 5… CONTINUE READING