Allosteric regulation and substrate activation in cytosolic nucleotidase II from Legionella pneumophila (pages 1613–1628)
Bharath Srinivasan, Farhad Forouhar, Arpit Shukla, Chethana Sampangi, Sonia Kulkarni, Mariam Abashidze, Jayaraman Seetharaman, Scott Lew, Lei Mao, Thomas B. Acton, Rong Xiao, John K. Everett, Gaetano T. Montelione, Liang Tong and Hemalatha Balaram
Version of Record online: 17 FEB 2014 | DOI: 10.1111/febs.12727
Legionella pneumophila cytosolic nucleotidase II (LpcN-II) hydrolyzes GMP, dGMP and IMP. GTP, GDP and the substrate GMP allosterically modulate LpcN-II activity. Crystal structures of LpcN-II revealed an activator binding site at the dimer interface, further confirmed by site-directed mutagenesis. Structural changes induced in LpcN-II tetramer upon activator binding may be the molecular mechanism of activation.