1h3d
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1h3d.gif|left|200px]]<br /><applet load="1h3d" size=" | + | [[Image:1h3d.gif|left|200px]]<br /><applet load="1h3d" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1h3d, resolution 2.7Å" /> | caption="1h3d, resolution 2.7Å" /> | ||
'''STRUCTURE OF THE E.COLI ATP-PHOSPHORIBOSYLTRANSFERASE'''<br /> | '''STRUCTURE OF THE E.COLI ATP-PHOSPHORIBOSYLTRANSFERASE'''<br /> | ||
| Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1H3D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with AMP and TLA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/ATP_phosphoribosyltransferase ATP phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.17 2.4.2.17] Known structural/functional Site: <scene name='pdbsite=AMP:Tla Binding Site For Chain A'>AMP</scene>. Full crystallographic information is available from [http:// | + | 1H3D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=AMP:'>AMP</scene> and <scene name='pdbligand=TLA:'>TLA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/ATP_phosphoribosyltransferase ATP phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.17 2.4.2.17] Known structural/functional Site: <scene name='pdbsite=AMP:Tla+Binding+Site+For+Chain+A'>AMP</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H3D OCA]. |
==Reference== | ==Reference== | ||
| Line 25: | Line 25: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:45:49 2008'' |
Revision as of 07:45, 3 February 2008
|
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 structures, indicates that histidine is solely responsible for the large, conformational changes observed between the hexameric forms of the enzyme., The role of oligomerisation in inhibition and the structural basis for the, synergistic inhibition by histidine and AMP are discussed.
About this Structure
1H3D is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as ATP phosphoribosyltransferase, with EC number 2.4.2.17 Known structural/functional Site: . 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 Sun Feb 3 09:45:49 2008
