Structure and dynamics of UDP-glucose pyrophosphorylase from Arabidopsis thaliana with bound UDP-glucose and UTP.

Structure and dynamics of UDP-glucose pyrophosphorylase from Arabidopsis thaliana with bound UDP-glucose and UTP. Research Abstract Details 

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Structure and dynamics of UDP-glucose pyrophosphorylase from Arabidopsis thaliana with bound UDP-glucose and UTP. Abstract Text:

Jason G McCoy,Eduard Bitto,Craig A Bingman,Gary E Wesenberg,Ryan M Bannen,Dmitry A Kondrashov,George N Phillips,

The structure of the UDP-glucose pyrophosphorylase encoded by Arabidopsis thaliana gene At3g03250 has been solved to a nominal resolution of 1.86 Angstroms. In addition, the structure has been solved in the presence of the substrates/products UTP and UDP-glucose to nominal resolutions of 1.64 Angstroms and 1.85 Angstroms. The three structures revealed a catalytic domain similar to that of other nucleotidyl-glucose pyrophosphorylases with a carboxy-terminal beta-helix domain in a unique orientation. Conformational changes are observed between the native and substrate-bound complexes. The nucleotide-binding loop and the carboxy-terminal domain, including the suspected catalytically important Lys360, move in and out of the active site in a concerted fashion. TLS refinement was employed initially to model conformational heterogeneity in the UDP-glucose complex followed by the use of multiconformer refinement for the entire molecule. Normal mode analysis generated atomic displacement predictions in good agreement in magnitude and direction with the observed conformational changes and anisotropic displacement parameters generated by TLS refinement. The structures and the observed dynamic changes provide insight into the ordered mechanism of this enzyme and previously described oligomerization effects on catalytic activity.

Structure and dynamics of UDP-glucose pyrophosphorylase from Arabidopsis thaliana with bound UDP-glucose and UTP. Publishing Authors By Initials

JG McCoy,E Bitto,CA Bingman,GE Wesenberg,RM Bannen,DA Kondrashov,GN Phillips,

For similar heterocyclic compounds: heterocyclic compounds, 1-ring: pyrimidines: pyrimidine nucleotides: uracil nucleotides: uridine triphosphate research abstracts see: heterocyclic compounds: heterocyclic compounds, 1-ring: pyrimidines: pyrimidine nucleotides: uracil nucleotides: uridine triphosphate research

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Structure and dynamics of UDP-glucose pyrophosphorylase from Arabidopsis thaliana with bound UDP-glucose and UTP. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Journal of molecular biology

VOLUME: 366

Page Numbers: 830-41

Journal Abbreviation: J. Mol. Biol.

ISSN: 0022-2836

DAY: 21

MONTH: 11

YEAR: 2006

Structure and dynamics of UDP-glucose pyrophosphorylase from Arabidopsis thaliana with bound UDP-glucose and UTP. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985088

Structure and dynamics of UDP-glucose pyrophosphorylase from Arabidopsis thaliana with bound UDP-glucose and UTP. Keywords Mesh Terms:

KEYWORDS: Uridine Triphosphate

MESH TERMS: metabolism

Chemical & Substance for Abstract: Structure and dynamics of UDP-glucose pyrophosphorylase from Arabidopsis thaliana with bound UDP-glucose and UTP. Information

Substance Name: UTP-Glucose-1-Phosphate Uridylyltransfer

Registry Number: EC 2.7.7.9

Grant and Affiliation Information for Structure and dynamics of UDP-glucose pyrophosphorylase from Arabidopsis thaliana with bound UDP-glucose and UTP.

AFFILIATION: Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.

Country: England

AGENCY: United States NIGMS

GRANT: U54 GM074901-01

ACRONYM: GM

MEDLINETA: J Mol Biol

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