1q1k

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[[Image:1q1k.jpg|left|200px]]
 
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{{Structure
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==Structure of ATP-phosphoribosyltransferase from E. coli complexed with PR-ATP==
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|PDB= 1q1k |SIZE=350|CAPTION= <scene name='initialview01'>1q1k</scene>, resolution 2.90&Aring;
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<StructureSection load='1q1k' size='340' side='right'caption='[[1q1k]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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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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<table><tr><td colspan='2'>[[1q1k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q1K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q1K FirstGlance]. <br>
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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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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
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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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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PRT:PHOSPHORIBOSYL+ATP'>PRT</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1q1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q1k OCA], [https://pdbe.org/1q1k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q1k RCSB], [https://www.ebi.ac.uk/pdbsum/1q1k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q1k ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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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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== Function ==
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}}
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[https://www.uniprot.org/uniprot/HIS1_ECOLI HIS1_ECOLI] Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.[HAMAP-Rule:MF_00079]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q1/1q1k_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1q1k ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''Structure of ATP-phosphoribosyltransferase from E. coli complexed with PR-ATP'''
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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<ref>PMID:14741209</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1q1k" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[ATP phosphoribosyl transferase 3D structures|ATP phosphoribosyl transferase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1Q1K is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q1K OCA].
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__TOC__
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</StructureSection>
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/14741209 14741209]
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[[Category: ATP phosphoribosyltransferase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Coggins, J R.]]
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[[Category: Coggins JR]]
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[[Category: Lapthorn, A J.]]
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[[Category: Lapthorn AJ]]
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[[Category: Lohkamp, B.]]
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[[Category: Lohkamp B]]
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[[Category: McDermott, G.]]
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[[Category: McDermott G]]
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[[Category: histidine biosynthesis]]
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[[Category: pr-atp inhibition]]
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[[Category: prpp binding]]
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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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Current revision

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

PDB ID 1q1k

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