1q1k: Difference between revisions

Revision as of 15:34, 21 February 2008

Structure of ATP-phosphoribosyltransferase from E. coli complexed with PR-ATP

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 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 StructureAbout this Structure

1Q1K 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 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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OCA

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-[[Image:1q1k.jpg|left|200px]]<br /><applet load="1q1k" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1q1k.jpg|left|200px]]<br /><applet load="1q1k" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1q1k, resolution 2.90&Aring;" />
 '''Structure of ATP-phosphoribosyltransferase from E. coli complexed with PR-ATP'''<br />
 ==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.
+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==
-Q1K 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 PRT 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q1K OCA].
+Q1K 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=PRT:'>PRT</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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q1K OCA].
 ==Reference==
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 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Coggins, J.R.]]
+[[Category: Coggins, J R.]]
-[[Category: Lapthorn, A.J.]]
+[[Category: Lapthorn, A J.]]
 [[Category: Lohkamp, B.]]
 [[Category: McDermott, G.]]
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 [[Category: prpp binding]]
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