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1jc5

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[[Image:1jc5.jpg|left|200px]]
 
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{{Structure
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==Crystal Structure of Native Methylmalonyl-CoA Epimerase==
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|PDB= 1jc5 |SIZE=350|CAPTION= <scene name='initialview01'>1jc5</scene>, resolution 2.20&Aring;
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<StructureSection load='1jc5' size='340' side='right'caption='[[1jc5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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<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>
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|ACTIVITY= [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]
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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]] 2.2&#8491;</td></tr>
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|GENE=
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<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>
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}}
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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=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>
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</table>
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'''Crystal Structure of Native Methylmalonyl-CoA Epimerase'''
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== Function ==
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[https://www.uniprot.org/uniprot/Q8VQN0_PROFR Q8VQN0_PROFR]
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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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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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jc/1jc5_consurf.spt"</scriptWhenChecked>
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1JC5 is a [[Single protein]] structure of sequence from [http://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].
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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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==Reference==
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</jmolCheckbox>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11470438 11470438]
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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].
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[[Category: Methylmalonyl-CoA epimerase]]
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Propionibacterium freudenreichii subsp. shermanii]]
[[Category: Propionibacterium freudenreichii subsp. shermanii]]
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[[Category: Single protein]]
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[[Category: Baker EN]]
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[[Category: Baker, E N.]]
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[[Category: Baker HM]]
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[[Category: Baker, H M.]]
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[[Category: Mc Carthy AA]]
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[[Category: Carthy, A A.Mc.]]
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[[Category: Patchett ML]]
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[[Category: Patchett, M L.]]
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[[Category: Shewry SC]]
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[[Category: Shewry, S C.]]
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[[Category: SO4]]
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[[Category: epimerisation]]
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:01:28 2008''
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Current revision

Crystal Structure of Native Methylmalonyl-CoA Epimerase

PDB ID 1jc5

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