Crystal structure and insights into the oligomeric state of UDP-glucose pyrophosphorylase from sugarcane

PloS One
Camila A CotrimMarcelo Menossi

Abstract

UDP-glucose pyrophosphorylase (UGPase) is found in all organisms and catalyses the formation of UDP-glucose. In sugarcane, UDP-glucose is a branch-point in the carbon channelling into other carbohydrates, such as sucrose and cellulose, which are the major factors for sugarcane productivity. In most plants, UGPase has been described to be enzymatically active in the monomeric form, while in human and yeast, homo-octamers represent the active form of the protein. Here, we present the crystal structure of UGPase from sugarcane (ScUGPase-1) at resolution of 2.0 Å. The crystals of ScUGPase-1 reveal the presence of two molecules in the asymmetric unit and the multi-angle light scattering analysis shows that ScUGPase-1 forms a mixture of species ranging from monomers to larger oligomers in solution, suggesting similarities with the orthologs from yeast and human.

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Citations

Nov 23, 2019·International Journal of Molecular Sciences·Antje KumpfDirk Tischler
Dec 10, 2020·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Satu Mikkola

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Methods Mentioned

BETA
X-ray
light scattering
x-ray scattering

Software Mentioned

Aimless ( CCP4 )
MUSCLE
AutoBuild wizard ( Phenix )
Protein interface and assemblies ” ( PISA )
PyMOL
Jalview
Astra6
Coot
Phaser
XDS

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