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Blackwell Science, LtdOxford, UKMMIMolecular Microbiology0950-382XBlackwell Publishing Ltd, 2004? 2004533829842Original ArticleSpo0A functional domainsK. Muchová et al

By K. Muchová, R. J. Lewis, D. Pere Ko, J. A. Brannigan, J. C. Ladds, A. Leech, A. J. Wilkinson and I. Barák

Abstract

Dimer-induced signal propagation in Spo0A Spo0A, the response regulator protein controlling the initiation of sporulation in Bacillus, has two distinct domains, an N-terminal phosphoacceptor (or receiver) domain and a C-terminal DNA-binding (or effector) domain. The phosphoacceptor domain mediates dimerization of Spo0A on phosphorylation. A comparison of the crystal structures of phosphorylated and unphosphorylated response regulators suggests a mechanism of activation in which structural changes originating at the phosphorylatable aspartate extend to the a 4b 5a 5 surface of the protein. In particular, the data show an important role in downstream signalling for a conserved aromatic residue (Phe-105 in Spo0A), the conformation of which alter

Year: 2013
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