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N-Acetyl-L-glutamate kinase from P. aeruginosa catalyses the controlling step of arginine biosynthesis and is feedback inhibited by arginine. The gene for this enzyme was cloned and expressed at high levels in E. coli. Crystals of the purified recombinant enzyme, belonging to space group P1, diffracted to a resolution of 2.75 Å.

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A large volume of electron density in the crystal of Escherichia coli N-acetyl-L-glutamate kinase is interpreted as an external AMPPNP molecule that makes contacts with the enzyme through its γ-imidophosphate. This external nucleotide differs in a number of respects from the internal AMPPNP bound to the active site, and the possibility that the external AMPPNP is waiting to occupy the active center is discussed.
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