This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1h3d
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1h3d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h3d, resolution 2.7Å" /> '''STRUCTURE OF THE E.C...)
Next diff →
Revision as of 17:14, 29 October 2007
|
STRUCTURE OF THE E.COLI ATP-PHOSPHORIBOSYLTRANSFERASE
Overview
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 Structure
1H3D is a [Single protein] structure of sequence from [Escherichia coli] with AMP and TLA as [ligands]. Active as [[1]], with EC number [2.4.2.17]. Full crystallographic information is available from [OCA].
Reference
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
Page seeded by OCA on Mon Oct 29 19:19:32 2007
