1eix

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(New page: 200px<br /><applet load="1eix" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eix, resolution 2.5&Aring;" /> '''STRUCTURE OF OROTIDIN...)
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[[Image:1eix.jpg|left|200px]]<br /><applet load="1eix" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1eix, resolution 2.5&Aring;" />
 
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'''STRUCTURE OF OROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE FROM E. COLI, CO-CRYSTALLISED WITH THE INHIBITOR BMP'''<br />
 
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==Overview==
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==STRUCTURE OF OROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE FROM E. COLI, CO-CRYSTALLISED WITH THE INHIBITOR BMP==
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Orotidine 5'-monophosphate decarboxylase (ODCase) catalyzes the, decarboxylation of orotidine 5'-monophosphate, the last step in the de, novo synthesis of uridine 5'-monophosphate. ODCase is a very proficient, enzyme [Radzicka, A., and Wolfenden, R. (1995) Science 267, 90-93], enhancing the reaction rate by a factor of 10(17). This proficiency has, been enigmatic, since it is achieved without metal ions or cofactors. Here, we present a 2.5 A resolution structure of ODCase complexed with the, inhibitor 1-(5'-phospho-beta-D-ribofuranosyl)barbituric acid. It shows a, closely packed dimer composed of two alpha/beta-barrels with two shared, active sites. The orientation of the orotate moiety of the substrate is, unambiguously deduced from the structure, and previously proposed, catalytic mechanisms involving protonation of O2 or O4 can be ruled out., The proximity of the OMP carboxylate group with Asp71 appears to be, instrumental for the decarboxylation of OMP, either through charge, repulsion or through the formation of a very short O.H.O hydrogen bond, between the two carboxylate groups.
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<StructureSection load='1eix' size='340' side='right'caption='[[1eix]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1eix]] is a 4 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=1EIX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EIX FirstGlance]. <br>
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1EIX 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 BMQ as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Orotidine-5'-phosphate_decarboxylase Orotidine-5'-phosphate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.23 4.1.1.23] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EIX OCA].
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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]] 2.5&#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=BMQ:1-(5-PHOSPHO-BETA-D-RIBOFURANOSYL)BARBITURIC+ACID'>BMQ</scene></td></tr>
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==Reference==
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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=1eix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eix OCA], [https://pdbe.org/1eix PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eix RCSB], [https://www.ebi.ac.uk/pdbsum/1eix PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eix ProSAT]</span></td></tr>
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Structural basis for the catalytic mechanism of a proficient enzyme: orotidine 5'-monophosphate decarboxylase., Harris P, Navarro Poulsen JC, Jensen KF, Larsen S, Biochemistry. 2000 Apr 18;39(15):4217-24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10757968 10757968]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PYRF_ECOLI PYRF_ECOLI] Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).[HAMAP-Rule:MF_01200_B]
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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/ei/1eix_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=1eix ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Orotidine-5'-phosphate decarboxylase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Harris P]]
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[[Category: Harris, P.]]
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[[Category: Jensen KF]]
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[[Category: Jensen, K.F.]]
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[[Category: Larsen S]]
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[[Category: Larsen, S.]]
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[[Category: Poulsen JCN]]
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[[Category: Poulsen, J.C.N.]]
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[[Category: BMQ]]
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[[Category: alpha-beta-barrel]]
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[[Category: homodimer]]
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[[Category: protein-inhibitor complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:02:12 2007''
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Current revision

STRUCTURE OF OROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE FROM E. COLI, CO-CRYSTALLISED WITH THE INHIBITOR BMP

PDB ID 1eix

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