Improved expression, purification and crystallization of a putative N-acetyl-gamma-glutamyl-phosphate reductase from rice (Oryza sativa)

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Jun Miura-OhnumaEtsuko Katoh

Abstract

N-Acetyl-gamma-glutamyl-phosphate reductase (AGPR) catalyzes the third step in an eight-step arginine-biosynthetic pathway that starts with glutamate. This enzyme converts N-acetyl-gamma-glutamyl phosphate to N-acetylglutamate-gamma-semialdehyde by an NADPH-dependent reductive dephosphorylation. AGPR from Oryza sativa (OsAGPR) was expressed in Escherichia coli at 291 K as a soluble fusion protein with an upstream thioredoxin-hexahistidine [Trx-(His)6] extension. OsAGPR(Ala50-Pro366) was purified and crystals were obtained using the sitting-drop vapour-diffusion method at 293 K and diffract X-rays to at least 1.8 A resolution. They belong to the hexagonal space group P6(1), with unit-cell parameters a = 86.11, c = 316.3 A.

References

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Mar 14, 2000·Current Opinion in Plant Biology·T Sasaki, B Burr
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Jan 30, 2003·Acta Crystallographica. Section D, Biological Crystallography·Masaru GotoKen Hirotsu
Jul 19, 2003·Science·UNKNOWN Rice Full-Length cDNA ConsortiumAyako Yasunishi
May 26, 2005·Protein Expression and Purification·Yuki TsunodaEtsuko Katoh

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Citations

Oct 3, 2006·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Fatemeh MoradianMichael N G James

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