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| ==Crystal Structure of Native Methylmalonyl-CoA Epimerase== | | ==Crystal Structure of Native Methylmalonyl-CoA Epimerase== |
| <StructureSection load='1jc5' size='340' side='right' caption='[[1jc5]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='1jc5' size='340' side='right'caption='[[1jc5]], [[Resolution|resolution]] 2.20Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[1jc5]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"propionibacterium_shermanii"_van_niel_1928 "propionibacterium shermanii" van niel 1928]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JC5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JC5 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[1jc5]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Propionibacterium_freudenreichii_subsp._shermanii Propionibacterium freudenreichii subsp. shermanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JC5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JC5 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.2Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jc4|1jc4]]</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylmalonyl-CoA_epimerase Methylmalonyl-CoA epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.99.1 5.1.99.1] </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=1jc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jc5 OCA], [https://pdbe.org/1jc5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jc5 RCSB], [https://www.ebi.ac.uk/pdbsum/1jc5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jc5 ProSAT]</span></td></tr> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jc5 OCA], [http://pdbe.org/1jc5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jc5 RCSB], [http://www.ebi.ac.uk/pdbsum/1jc5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jc5 ProSAT]</span></td></tr> | |
| </table> | | </table> |
| | == Function == |
| | [https://www.uniprot.org/uniprot/Q8VQN0_PROFR Q8VQN0_PROFR] |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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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=1jc5 ConSurf]. | | </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=1jc5 ConSurf]. |
| <div style="clear:both"></div> | | <div style="clear:both"></div> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| BACKGROUND: Methylmalonyl-CoA epimerase (MMCE) is an essential enzyme in the breakdown of odd-numbered fatty acids and of the amino acids valine, isoleucine, and methionine. Present in many bacteria and in animals, it catalyzes the conversion of (2R)-methylmalonyl-CoA to (2S)-methylmalonyl-CoA, the substrate for the B12-dependent enzyme, methylmalonyl-CoA mutase. Defects in this pathway can result in severe acidosis and cause damage to the central nervous system in humans. RESULTS: The crystal structure of MMCE from Propionibacterium shermanii has been determined at 2.0 A resolution. The MMCE monomer is folded into two tandem betaalphabetabetabeta modules that pack edge-to-edge to generate an 8-stranded beta sheet. Two monomers then pack back-to-back to create a tightly associated dimer. In each monomer, the beta sheet curves around to create a deep cleft, in the floor of which His12, Gln65, His91, and Glu141 provide a binding site for a divalent metal ion, as shown by the binding of Co2+. Modeling 2-methylmalonate into the active site identifies two glutamate residues as the likely essential bases for the epimerization reaction. CONCLUSIONS: The betaalphabetabetabeta modules of MMCE correspond with those found in several other proteins, including bleomycin resistance protein, glyoxalase I, and a family of extradiol dioxygenases. Differences in connectivity are consistent with the evolution of these very different proteins from a common precursor by mechanisms of gene duplication and domain swapping. The metal binding residues also align precisely, and striking structural similarities between MMCE and glyoxalase I suggest common mechanisms in their respective epimerization and isomerization reactions.
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| Crystal structure of methylmalonyl-coenzyme A epimerase from P. shermanii: a novel enzymatic function on an ancient metal binding scaffold.,McCarthy AA, Baker HM, Shewry SC, Patchett ML, Baker EN Structure. 2001 Jul 3;9(7):637-46. PMID:11470438<ref>PMID:11470438</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 1jc5" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Propionibacterium shermanii van niel 1928]] | | [[Category: Large Structures]] |
| [[Category: Methylmalonyl-CoA epimerase]] | | [[Category: Propionibacterium freudenreichii subsp. shermanii]] |
| [[Category: Baker, E N]] | | [[Category: Baker EN]] |
| [[Category: Baker, H M]] | | [[Category: Baker HM]] |
| [[Category: Carthy, A A.Mc]] | | [[Category: Mc Carthy AA]] |
| [[Category: Patchett, M L]] | | [[Category: Patchett ML]] |
| [[Category: Shewry, S C]] | | [[Category: Shewry SC]] |
| [[Category: Epimerisation]]
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| [[Category: Isomerase]]
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| [[Category: Metal-assisted catalysis]]
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| [[Category: Methylmalonyl-coa]]
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| [[Category: Vicinal oxygen chelate superfamily]]
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