scholarly journals Crystallization and x-ray diffraction studies of a phosphate-binding protein involved in active transport in Escherichia coli.

1986 ◽  
Vol 261 (17) ◽  
pp. 7995-7996
Author(s):  
B D Kubena ◽  
H Luecke ◽  
H Rosenberg ◽  
F A Quiocho
Keyword(s):  
Escherichia Coli ◽  
Active Transport ◽  
Binding Protein ◽  
X Ray Diffraction ◽  
Phosphate Binding ◽  
X Ray ◽  
Phosphate Binding Protein

scholarly journals Crystallization and preliminary X-ray diffraction analysis of human phosphate-binding protein

2005 ◽  
Vol 62 (1) ◽  
pp. 67-69 ◽  
Author(s):  
Carlos Contreras-Martel ◽  
Philippe Carpentier ◽  
Renaud Morales ◽  
Frédérique Renault ◽  
Marie-Laure Chesne-Seck ◽  
...  
Keyword(s):  
Diffraction Analysis ◽  
Binding Protein ◽  
X Ray Diffraction ◽  
Phosphate Binding ◽  
X Ray ◽  
Phosphate Binding Protein

scholarly journals Crystallization and preliminary X-ray diffraction analysis of the phosphate-binding protein PhoX fromXanthomonas citri

2014 ◽  
Vol 70 (12) ◽  
pp. 1604-1607 ◽  
Author(s):  
Vanessa R. Pegos ◽  
Francisco Javier Medrano ◽  
Andrea Balan
Keyword(s):  
Binding Protein ◽  
Structural Data ◽  
Citrus Canker ◽  
Economic Losses ◽  
X Ray Diffraction ◽  
Phosphate Binding ◽  
Canker Disease ◽  
X Ray ◽  
Periplasmic Binding Proteins ◽  
Phosphate Binding Protein

Xanthomonas axonopodispv.citri(X. citri) is an important bacterium that causes citrus canker disease in plants in Brazil and around the world, leading to significant economic losses. Determination of the physiology and mechanisms of pathogenesis of this bacterium is an important step in the development of strategies for its containment. Phosphate is an essential ion in all microrganisms owing its importance during the synthesis of macromolecules and in gene and protein regulation. Interestingly,X. citrihas been identified to present two periplasmic binding proteins that have not been further characterized: PstS, from an ATP-binding cassette for high-affinity uptake and transport of phosphate, and PhoX, which is encoded by an operon that also contains a putative porin for the transport of phosphate. Here, the expression, purification and crystallization of the phosphate-binding protein PhoX and X-ray data collection at 3.0 Å resolution are described. Biochemical, biophysical and structural data for this protein will be helpful in the elucidation of its function in phosphate uptake and the physiology of the bacterium.

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