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Structural studies of tri-functional human GART.

Martin Welin¹, Jörg Günter Grossmann, Susanne Flodin

¹Structural Genomics Consortium, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-17177 Stockholm, Sweden.

Nucleic Acids Research

|July 16, 2010

Summary

The human purine de novo synthesis enzyme GART has a unique seesaw shape, facilitating its function. Structural analysis reveals insights into its catalytic mechanism and dimeric formation.

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Area of Science:

Biochemistry
Structural Biology
Enzymology

Background:

The purine de novo synthesis pathway is essential for cell viability.
GART (glycinamide ribonucleotide synthetase, GAR transformylase, and IMP cyclohydrolase) is a key multi-functional enzyme in this pathway.

Purpose of the Study:

To elucidate the structural basis of GART's enzymatic activities.
To understand the quaternary structure and dynamics of full-length GART.

Main Methods:

X-ray crystallography was used to determine the structures of two GART domains.
Small-angle X-ray scattering (SAXS) was employed to model the full-length GART protein.

Main Results:

Structures of the glycinamide ribonucleotide synthetase and aminoimidazole ribonucleotide synthetase domains were solved and compared to prokaryotic homologs.
SAXS models indicate GART forms a dimer through its middle domain, adopting a flexible, seesaw-like conformation.
Flexible linkers allow high mobility of the terminal enzyme units.

Conclusions:

The unique seesaw structure of GART may facilitate efficient substrate channeling within the enzyme or to other pathway enzymes.
Understanding GART structure provides insights into purine biosynthesis regulation and potential therapeutic targets.