1ao0
From Proteopedia
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GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) AMIDOTRANSFERASE FROM B. SUBTILIS COMPLEXED WITH ADP AND GMP
Overview
De novo purine nucleotide synthesis is regulated, at least in part, by, end-product inhibition of glutamine PRPP amidotransferase. An important, feature of this inhibition is the fact that certain synergistic nucleotide, pairs give more than additive inhibition. The physiological importance of, synergism is in amplifying regulation by the adenine and guanine, nucleotide end products of de novo synthesis. Using a new method to, quantitate synergism, ADP plus GMP were confirmed [Meyer, E., and Switzer, R. L. (1978) J. Biol. Chem. 254, 5397-5402] to give strong synergistic, inhibition of Bacillus subtilis glutamine PRPP amidotransferase. An X-ray, structure of the ternary enzyme.ADP.GMP complex established that ADP binds, to the allosteric A site and GMP to the catalytic C site. GMP ... [(full description)]
About this Structure
1AO0 is a [Single protein] structure of sequence from [Bacillus subtilis] with MG, SF4, 5GP and ADP as [ligands]. Active as [[1]], with EC number [2.4.2.14]. Full crystallographic information is available from [OCA].
Reference
Mechanism of the synergistic end-product regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase by nucleotides., Chen S, Tomchick DR, Wolle D, Hu P, Smith JL, Switzer RL, Zalkin H, Biochemistry. 1997 Sep 2;36(35):10718-26. PMID:9271502
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