TAILIEUCHUNG - Báo cáo khoa học: Structure of Streptococcus agalactiae serine⁄threonine phosphatase The subdomain conformation is coupled to the binding of a third metal ion

We solved the crystal structure ofStreptococcus agalactiaeserine⁄threonine phosphatase (SaSTP) using a combination of single-wavelength anomalous dispersion phasing and molecular replacement. The overall structure resem-bles that of previously characterized members of the PPM⁄PP2C STP fam-ily. | ễFEBS Journal Structure of Streptococcus agalactiae serine threonine phosphatase The subdomain conformation is coupled to the binding of a third metal ion Mika K. Rantanen1 Lari Lehtio1 Lakshmi Rajagopal2 Craig E. Rubens2 and Adrian Goldman1 1 Institute of Biotechnology University of Helsinki Finland 2 Division of Infectious Disease Children s Hospitaland RegionalMedicalCenter Seattle WA USA Keywords dephosphorylation serine threonine phosphatase signaling Streptococcus agalactiae structure Correspondence A. Goldman Institute of Biotechnology University of Helsinki PO Box 65 00014 Helsinki Finland Fax 358 9191 59940 Tel 358 9191 58923 E-mail Received 31 January 2007 revised 20 April 2007 accepted 25 April 2007 doi We solved the crystal structure of Streptococcus agalactiae serine threonine phosphatase SaSTP using a combination of single-wavelength anomalous dispersion phasing and molecular replacement. The overall structure resembles that of previously characterized members of the PPM PP2C STP family. The asymmetric unit contains four monomers and we observed two novel conformations for the flap domain among them. In one of these conformations the enzyme binds three metal ions whereas in the other it binds only two. The three-metal ion structure also has the active site arginine in a novel conformation. The switch between the two- and three-metal ion structures appears to be binding of another monomer to the active site of STP which promotes binding of the third metal ion. This interaction may mimic the binding of a product complex especially since the motif binding to the active site contains a serine residue aligning remarkably well with the phosphate found in the human STP structure. Protein phosphatases are primarily classified on the basis of the type of the amino acid they dephosphorylate serine threonine phosphatases STPs act specifically on phosphoserine and phosphothreonine residues. Evolution has

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