1h3d: Difference between revisions
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Revision as of 16:22, 30 October 2007
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STRUCTURE OF THE E.COLI ATP-PHOSPHORIBOSYLTRANSFERASE
OverviewOverview
ATP-phosphoribosyltransferase (ATP-PRT), the first enzyme of the histidine, pathway, is a complex allosterically regulated enzyme, which controls the, flow of intermediates through this biosynthetic pathway. The crystal, structures of Escherichia coli ATP-PRT have been solved in complex with, the inhibitor AMP at 2.7A and with product PR-ATP at 2.9A (the, ribosyl-triphosphate could not be resolved). On the basis of binding of, AMP and PR-ATP and comparison with type I PRTs, the PRPP and parts of the, ATP-binding site are identified. These structures clearly identify the AMP, as binding in the 5-phosphoribosyl-alpha-1-pyrophosphate (PRPP)-binding, site, with the adenosine ring occupying the ATP-binding site. Comparison, with the recently solved Mycobacterium tuberculosis ATP-PRT ... [(full description)]
About this StructureAbout this Structure
1H3D is a [Single protein] structure of sequence from [Escherichia coli] with AMP and TLA as [ligands]. Active as [ATP phosphoribosyltransferase], with EC number [2.4.2.17]. Structure known Active Site: AMP. Full crystallographic information is available from [OCA].
ReferenceReference
The structure of Escherichia coli ATP-phosphoribosyltransferase: identification of substrate binding sites and mode of AMP inhibition., Lohkamp B, McDermott G, Campbell SA, Coggins JR, Lapthorn AJ, J Mol Biol. 2004 Feb 6;336(1):131-44. PMID:14741209
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