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

Camila A Cotrim; Jose Sergio M Soares; Bostjan Kobe; Marcelo Menossi

doi:10.1371/journal.pone.0193667

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

PLoS One. 2018 Mar 1;13(3):e0193667. doi: 10.1371/journal.pone.0193667. eCollection 2018.

Authors

Camila A Cotrim¹, Jose Sergio M Soares², Bostjan Kobe¹, Marcelo Menossi²

Affiliations

¹ School of Chemistry and Molecular Bioscience and Australia Infectious Diseases Research Centre, University of Queensland, Brisbane, Queensland, Australia.
² Departamento de Genética, Evolução, Microbiologia e Imunologia, Instituto de Biologia, Universidade Estadual de Campinas, Campinas, São Paulo, Brazil.

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Catalytic Domain
Cloning, Molecular
Crystallography, X-Ray
Models, Molecular
Plant Proteins / chemistry
Plant Proteins / genetics
Plant Proteins / metabolism
Protein Conformation
Protein Multimerization
Saccharum / chemistry
Saccharum / enzymology*
Saccharum / genetics
UTP-Glucose-1-Phosphate Uridylyltransferase / chemistry*
UTP-Glucose-1-Phosphate Uridylyltransferase / genetics*
UTP-Glucose-1-Phosphate Uridylyltransferase / metabolism

Substances

Plant Proteins
UTP-Glucose-1-Phosphate Uridylyltransferase

Grants and funding

This work was supported by Grant 2013/15576-5 - Fundação de Amparo à Pesquisa do Estado de São Paulo - http://www.fapesp.br/ to MM; grant 2008/06767-3 - Fundação de Amparo à Pesquisa do Estado de São Paulo - http://www.fapesp.br/ to JSMS. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.