Structure-function relationships in a bacterial DING protein

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

Research output: Contribution to journalArticlepeer-review

29 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 languageEnglish (US)
Pages (from-to)3455-3460
Number of pages6
JournalFEBS Letters
Volume581
Issue number18
DOIs
StatePublished - 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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