2pk0
Structure of the S. agalactiae serine/threonine phosphatase at 2.65 resolution
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OverviewOverview
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.
About this StructureAbout this Structure
2PK0 is a Single protein structure of sequence from Streptococcus agalactiae with , and as ligands. Active as Phosphoprotein phosphatase, with EC number 3.1.3.16 Full crystallographic information is available from OCA.
ReferenceReference
Structure of Streptococcus agalactiae serine/threonine phosphatase. The subdomain conformation is coupled to the binding of a third metal ion., Rantanen MK, Lehtio L, Rajagopal L, Rubens CE, Goldman A, FEBS J. 2007 Jun;274(12):3128-37. Epub 2007 May 22. PMID:17521332
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