4.5 Article

Structure-function. relationships in a bacterial DING protein

Journal

FEBS LETTERS
Volume 581, Issue 18, Pages 3455-3460

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2007.06.050

Keywords

DING protein; phosphate binding; human phosphate-binding protein; pstS protein

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A recombinant DING protein from Pseudomonas fluorescens has been previously shown to have a phosphate-binding site, and to be mitogenic for human cells. Here we report the three-dimensional structure of the protein, confirming a close similarity to the Venus flytrap structure seen in other human and bacterial phosphate-binding proteins. Site-directed mutagenesis confirms the role of a key residue involved in phosphate binding, and that the mitogenic activity is not dependent on this property. Deletion of one of the two hinged domains that constitute the Venus flytrap also eliminates phosphate binding whilst enhancing mitogenic activity. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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