1l2u

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{{Seed}}
 
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[[Image:1l2u.png|left|200px]]
 
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==Orotidine 5'-monophosphate decarboxylase from E. coli==
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The line below this paragraph, containing "STRUCTURE_1l2u", creates the "Structure Box" on the page.
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<StructureSection load='1l2u' size='340' side='right'caption='[[1l2u]], [[Resolution|resolution]] 2.50&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'>[[1l2u]] is a 2 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=1L2U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L2U FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1l2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l2u OCA], [https://pdbe.org/1l2u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l2u RCSB], [https://www.ebi.ac.uk/pdbsum/1l2u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l2u ProSAT]</span></td></tr>
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{{STRUCTURE_1l2u| PDB=1l2u | SCENE= }}
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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/l2/1l2u_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=1l2u 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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Orotidine 5'-monophosphate decarboxylase (ODCase) catalyses the decarboxylation of orotidine 5'-monophosphate to uridine 5'-monophosphate (UMP). We have earlier determined the structure of ODCase from Escherichia coli complexed with the inhibitor 1-(5'-phospho-beta-d-ribofuranosyl)barbituric acid (BMP); here we present the 2.5 A structure of the uncomplexed apo enzyme, determined from twinned crystals. A structural analysis and comparison of the two structures of the E. coli enzyme show that binding of the inhibitor is accompanied by significant domain movements of approximately 12 degrees around a hinge that crosses the active site. Hence, the ODCase dimer, which contains two active sites, may be divided in three domains: a central domain that is fixed, and two lids which independently move 12 degrees upon binding. Corresponding analyses, presented herein, of the two Saccharomyces cerevisiae ODCase structures (with and without BMP) and the Methanobacterium thermoautotrophicum ODCase structures (with and without 6-aza UMP) show very similar, but somewhat smaller domain movements. The domain movements seem to be initiated by the phosphoryl binding to the enzyme and can explain why the binding of the phosphoryl group is essential for the catalytic function.
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===Orotidine 5'-monophosphate decarboxylase from E. coli===
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Substrate binding induces domain movements in orotidine 5'-monophosphate decarboxylase.,Harris P, Poulsen JC, Jensen KF, Larsen S J Mol Biol. 2002 May 10;318(4):1019-29. PMID:12054799<ref>PMID:12054799</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 1l2u" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12054799}}, adds the Publication Abstract to the page
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*[[Uridine 5'-monophosphate synthase 3D structures|Uridine 5'-monophosphate synthase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 12054799 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12054799}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1L2U 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=1L2U OCA].
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==Reference==
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Substrate binding induces domain movements in orotidine 5'-monophosphate decarboxylase., Harris P, Poulsen JC, Jensen KF, Larsen S, J Mol Biol. 2002 May 10;318(4):1019-29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12054799 12054799]
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[[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 JC]]
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[[Category: Poulsen, J C.]]
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[[Category: Beta-alpha-barrel]]
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[[Category: Homodimer]]
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[[Category: Twinned crystal]]
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[[Category: X-ray diffraction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:34:49 2008''
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Current revision

Orotidine 5'-monophosphate decarboxylase from E. coli

PDB ID 1l2u

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