2q9t
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High-resolution structure of the DING protein from Pseudomonas fluorescens
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Structural highlights
FunctionEvolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedA 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. Structure-function relationships in a bacterial DING protein.,Ahn S, Moniot S, Elias M, Chabriere E, Kim D, Scott K FEBS Lett. 2007 Jul 24;581(18):3455-60. Epub 2007 Jun 27. PMID:17612529[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 11:26, 30 August 2023.