Ontology highlight
ABSTRACT:
SUBMITTER: Saalau-Bethell SM
PROVIDER: S-EPMC4506562 | biostudies-literature | 2014 Apr
REPOSITORIES: biostudies-literature
Saalau-Bethell Susanne M SM Berdini Valerio V Cleasby Anne A Congreve Miles M Coyle Joseph E JE Lock Victoria V Murray Christopher W CW O'Brien M Alistair MA Rich Sharna J SJ Sambrook Tracey T Vinkovic Mladen M Yon Jeff R JR Jhoti Harren H
ChemMedChem 20140224 4
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' ...[more]