Structure-function. relationships in a bacterial DING protein

被引:29
|
作者
Ahn, Soyeon
Moniot, Sebastien
Elias, Mikael
Chabriere, Eric
Kim, Donghyo
Scott, Ken [1 ]
机构
[1] Univ Auckland, Sch Biol Sci, Auckland, New Zealand
[2] Univ Henri Poincare, Lab Cristallog & Modelisat Mat, CNRS, F-54506 Vandoeuvre Les Nancy, France
关键词
DING protein; phosphate binding; human phosphate-binding protein; pstS protein;
D O I
10.1016/j.febslet.2007.06.050
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:3455 / 3460
页数:6
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