1ecj
From Proteopedia
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ESCHERICHIA COLI GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) AMIDOTRANSFERASE COMPLEXED WITH 2 AMP PER TETRAMER
Overview
Crystal structures of glutamine phosphoribosylpyrophosphate (PRPP), amidotransferase from Escherichia coli have been determined to 2.0-A, resolution in the absence of ligands, and to 2.5-A resolution with the, feedback inhibitor AMP bound to the PRPP catalytic site. Glutamine PRPP, amidotransferase (GPATase) employs separate catalytic domains to abstract, nitrogen from the amide of glutamine and to transfer nitrogen to the, acceptor substrate PRPP. The unliganded and AMP-bound structures, which, are essentially identical, are interpreted as the inhibited form of the, enzyme because the two active sites are disconnected and the PRPP active, site is solvent exposed. The structures were compared with a previously, reported 3.0-A structure of the homologous Bacillus subtilis enzyme (Smith, JL ... [(full description)]
About this Structure
1ECJ is a [Single protein] structure of sequence from [Escherichia coli] with AMP as [ligand]. Active as [[1]], with EC number [2.4.2.14]. Full crystallographic information is available from [OCA].
Reference
Crystal structure of glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli., Muchmore CR, Krahn JM, Kim JH, Zalkin H, Smith JL, Protein Sci. 1998 Jan;7(1):39-51. PMID:9514258
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