2ate

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[[Image:2ate.png|left|200px]]
 
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==Structure of the complex of PurE with NitroAIR==
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The line below this paragraph, containing "STRUCTURE_2ate", creates the "Structure Box" on the page.
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<StructureSection load='2ate' size='340' side='right'caption='[[2ate]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2ate]] 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=2ATE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ATE FirstGlance]. <br>
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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]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NIA:((2R,3S,4R,5R)-5-(5-AMINO-4-NITRO-1H-IMIDAZOL-1-YL)-3,4-DIHYDROXYTETRAHYDROFURAN-2-YL)METHYL+DIHYDROGEN+PHOSPHATE'>NIA</scene></td></tr>
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{{STRUCTURE_2ate| PDB=2ate | SCENE= }}
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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=2ate FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ate OCA], [https://pdbe.org/2ate PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ate RCSB], [https://www.ebi.ac.uk/pdbsum/2ate PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ate ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PURE_ECOLI PURE_ECOLI] Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
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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/at/2ate_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2ate 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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N5-Carboxyaminoimidazole ribonucleotide mutase (N5-CAIR mutase or PurE) from Escherichia coli catalyzes the reversible interconversion of N5-CAIR to carboxyaminoimidazole ribonucleotide (CAIR) with direct CO2 transfer. Site-directed mutagenesis, a pH-rate profile, DFT calculations, and X-ray crystallography together provide new insight into the mechanism of this unusual transformation. These studies suggest that a conserved, protonated histidine (His45) plays an essential role in catalysis. The importance of proton transfers is supported by DFT calculations on CAIR and N5-CAIR analogues in which the ribose 5'-phosphate is replaced with a methyl group. The calculations suggest that the nonaromatic tautomer of CAIR (isoCAIR) is only 3.1 kcal/mol higher in energy than its aromatic counterpart, implicating this species as a potential intermediate in the PurE-catalyzed reaction. A structure of wild-type PurE cocrystallized with 4-nitroaminoimidazole ribonucleotide (NO2-AIR, a CAIR analogue) and structures of H45N and H45Q PurEs soaked with CAIR have been determined and provide the first insight into the binding of an intact PurE substrate. A comparison of 19 available structures of PurE and PurE mutants in apo and nucleotide-bound forms reveals a common, buried carboxylate or CO2 binding site for CAIR and N5-CAIR in a hydrophobic pocket in which the carboxylate or CO2 interacts with backbone amides. This work has led to a mechanistic proposal in which the carboxylate orients the substrate for proton transfer from His45 to N5-CAIR to form an enzyme-bound aminoimidazole ribonucleotide (AIR) and CO2 intermediate. Subsequent movement of the aminoimidazole moiety of AIR reorients it for addition of CO2 at C4 to generate isoCAIR. His45 is now in a position to remove a C4 proton to produce CAIR.
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===Structure of the complex of PurE with NitroAIR===
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N5-CAIR mutase: role of a CO2 binding site and substrate movement in catalysis.,Hoskins AA, Morar M, Kappock TJ, Mathews II, Zaugg JB, Barder TE, Peng P, Okamoto A, Ealick SE, Stubbe J Biochemistry. 2007 Mar 13;46(10):2842-55. Epub 2007 Feb 14. PMID:17298082<ref>PMID:17298082</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 2ate" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_17298082}}, adds the Publication Abstract to the page
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*[[Phosphoribosylaminoimidazole carboxylase 3D structures|Phosphoribosylaminoimidazole carboxylase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 17298082 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17298082}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[2ate]] is a 1 chain structure with 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=2ATE OCA].
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==Reference==
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<ref group="xtra">PMID:17298082</ref><ref group="xtra">PMID:11006546</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Phosphoribosylaminoimidazole carboxylase]]
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[[Category: Large Structures]]
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[[Category: Ealick, S E.]]
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[[Category: Ealick SE]]
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[[Category: Hoskins, A A.]]
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[[Category: Hoskins AA]]
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[[Category: Kappock, T J.]]
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[[Category: Kappock TJ]]
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[[Category: Mathews, I I.]]
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[[Category: Mathews II]]
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[[Category: Okamoto, A.]]
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[[Category: Okamoto A]]
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[[Category: Peng, P.]]
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[[Category: Peng P]]
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[[Category: Stubbe, J.]]
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[[Category: Stubbe J]]
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[[Category: Zaugg, J B.]]
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[[Category: Zaugg JB]]
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[[Category: Lyase]]
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[[Category: Nitroair complex]]
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[[Category: Pure]]
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Current revision

Structure of the complex of PurE with NitroAIR

PDB ID 2ate

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