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Crystallization, diffraction data collection and preliminary crystallographic analysis of DING protein from Pseudomonas fluorescens.

Authors :
Moniot, Sebastien
Elias, Mikael
Kim, Donghyo
Scott, Ken
Chabriere, Eric
Source :
Acta Crystallographica: Section F (Wiley-Blackwell). Jul2007, Vol. 63 Issue 7, p590-592. 3p. 2 Diagrams, 1 Chart.
Publication Year :
2007

Abstract

PfluDING is a phosphate-binding protein expressed in Pseudomonas fluorescens. This protein is clearly distinct from the bacterial ABC transporter soluble phosphate-binding protein PstS and is more homologous to eukaryotic DING proteins. Interestingly, bacterial DING proteins have only been detected in certain Pseudomonas species. Although DING proteins seem to be ubiquitous in eukaryotes, they are systematically absent from eukaryotic genomic databases and thus are still quite mysterious and poorly characterized. PfluDING displays mitogenic activity towards human cells and binds various ligands such as inorganic phosphate, pyrophosphate, nucleotide triphosphates and cotinine. Here, the crystallization of PfluDING is reported in a monoclinic space group ( P21), with typical unit-cell parameters a = 36.7, b = 123.7, c = 40.8 Å, α = 90, β = 116.7, γ = 90°. Preliminary crystallographic analysis reveals good diffraction quality for these crystals and a 1.43 Å resolution data set has been collected. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
17443091
Volume :
63
Issue :
7
Database :
Academic Search Index
Journal :
Acta Crystallographica: Section F (Wiley-Blackwell)
Publication Type :
Academic Journal
Accession number :
25654024
Full Text :
https://doi.org/10.1107/S1744309107028102