Publication Abstract from PubMed
Streptococcus agalactiae, a prokaryote that causes infections in neonates and immunocompromised adults, has a serine/threonine protein kinase (STK) signalling cascade. The structure of one of the targets, a family II inorganic pyrophosphatase, has been solved by molecular replacement and refined at 2.80 A resolution to an R factor of 19.2% (R(free) = 26.7%). The two monomers in the asymmetric unit are related by a noncrystallographic twofold axis, but the biological dimer is formed by a crystallographic twofold. Each monomer contains the pyrophosphate analogue imidodiphosphate (PNP) and three metal ions per active site: two Mn(2+) ions in sites M1 and M2 and an Mg(2+) ion in site M3. The enzyme is in the closed conformation. Like other family II enzymes, the structure consists of two domains (residues 1-191 and 198-311), with the active site located between them. The conformation of Lys298 in the active site is different from those observed previously and it coordinates to the conserved DHH motif in a unique way. The structure suggests that Ser150, Ser194, Ser195 and Ser296 are the most likely targets for the Ser/Thr kinase and phosphatase because they are surface-accessible and either in the active site or in the hinge region between the two domains.
Structure of the Streptococcus agalactiae family II inorganic pyrophosphatase at 2.80 A resolution.,Rantanen MK, Lehtio L, Rajagopal L, Rubens CE, Goldman A Acta Crystallogr D Biol Crystallogr. 2007 Jun;63(Pt 6):738-43. Epub 2007, May 15. PMID:17505113[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
