1q1k

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[[Image:1q1k.jpg|left|200px]]
[[Image:1q1k.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1q1k |SIZE=350|CAPTION= <scene name='initialview01'>1q1k</scene>, resolution 2.90&Aring;
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The line below this paragraph, containing "STRUCTURE_1q1k", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=PRT:PHOSPHORIBOSYL+ATP'>PRT</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= HISG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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-->
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|DOMAIN=
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{{STRUCTURE_1q1k| PDB=1q1k | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q1k OCA], [http://www.ebi.ac.uk/pdbsum/1q1k PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q1k RCSB]</span>
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}}
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'''Structure of ATP-phosphoribosyltransferase from E. coli complexed with PR-ATP'''
'''Structure of ATP-phosphoribosyltransferase from E. coli complexed with PR-ATP'''
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[[Category: Lohkamp, B.]]
[[Category: Lohkamp, B.]]
[[Category: McDermott, G.]]
[[Category: McDermott, G.]]
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[[Category: histidine biosynthesis]]
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[[Category: Histidine biosynthesis]]
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[[Category: pr-atp inhibition]]
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[[Category: Pr-atp inhibition]]
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[[Category: prpp binding]]
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[[Category: Prpp binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:45:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:07:32 2008''
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Revision as of 02:45, 3 May 2008

Template:STRUCTURE 1q1k

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


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

1Q1K is a Single protein structure of sequence from Escherichia coli. 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 Sat May 3 05:45:12 2008

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