Structure-function relationships in a bacterial DING protein

Soyeon Ahn; Sebastien Moniot; Mikael Elias; Eric Chabriere; Donghyo Kim; Ken Scott

doi:10.1016/j.febslet.2007.06.050

Structure-function relationships in a bacterial DING protein

Soyeon Ahn, Sebastien Moniot, Mikael Elias, Eric Chabriere, Donghyo Kim, Ken Scott

Biochemistry, Molecular Biology, and Biophysics (CBS)

Research output: Contribution to journal › Article › peer-review

30 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	3455-3460
Number of pages	6
Journal	FEBS Letters
Volume	581
Issue number	18
DOIs	https://doi.org/10.1016/j.febslet.2007.06.050
State	Published - Jul 24 2007

Bibliographical note

Funding Information:
We thank Manasa Ramakrishna for assistance with the running of the SP 3 structure prediction programme, to model truncated variants of PfluDING. Financial support was provided by the University of Auckland Staff Research Fund.

Keywords

DING protein
Human phosphate-binding protein
Phosphate binding
pstS protein

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AU - Moniot, Sebastien

AU - Elias, Mikael

AU - Chabriere, Eric

AU - Kim, Donghyo

AU - Scott, Ken

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Structure-function relationships in a bacterial DING protein

Abstract

Bibliographical note

Keywords

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