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| | <StructureSection load='1l2u' size='340' side='right'caption='[[1l2u]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='1l2u' size='340' side='right'caption='[[1l2u]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1l2u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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> | + | <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> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1eix|1eix]], [[1jjk|1jjk]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Orotidine-5'-phosphate_decarboxylase Orotidine-5'-phosphate decarboxylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.23 4.1.1.23] </span></td></tr>
| + | |
| | <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> | | <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> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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]
| + | [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] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Orotidine-5'-phosphate decarboxylase]]
| + | [[Category: Harris P]] |
| - | [[Category: Harris, P]] | + | [[Category: Jensen KF]] |
| - | [[Category: Jensen, K F]] | + | [[Category: Larsen S]] |
| - | [[Category: Larsen, S]] | + | [[Category: Poulsen JC]] |
| - | [[Category: Poulsen, J C]] | + | |
| - | [[Category: Beta-alpha-barrel]]
| + | |
| - | [[Category: Homodimer]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Twinned crystal]]
| + | |
| Structural highlights
Function
PYRF_ECOLI Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).[HAMAP-Rule:MF_01200_B]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Harris P, Poulsen JC, Jensen KF, Larsen S. Substrate binding induces domain movements in orotidine 5'-monophosphate decarboxylase. J Mol Biol. 2002 May 10;318(4):1019-29. PMID:12054799 doi:10.1016/S0022-2836(02)00200-0
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