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==Crystal Structure of Native Methylmalonyl-CoA Epimerase==
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<StructureSection load='1jc5' size='340' side='right'caption='[[1jc5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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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</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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<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>
{{STRUCTURE_1jc5|  PDB=1jc5  |  SCENE= }}
<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>
 
</table>
'''Crystal Structure of Native Methylmalonyl-CoA Epimerase'''
== Function ==
 
[https://www.uniprot.org/uniprot/Q8VQN0_PROFR Q8VQN0_PROFR]
 
== Evolutionary Conservation ==
==Overview==
[[Image:Consurf_key_small.gif|200px|right]]
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.
Check<jmol>
 
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==About this Structure==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jc/1jc5_consurf.spt"</scriptWhenChecked>
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].  
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==Reference==
  </jmolCheckbox>
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]
</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].
[[Category: Methylmalonyl-CoA epimerase]]
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Propionibacterium freudenreichii subsp. shermanii]]
[[Category: Propionibacterium freudenreichii subsp. shermanii]]
[[Category: Single protein]]
[[Category: Baker EN]]
[[Category: Baker, E N.]]
[[Category: Baker HM]]
[[Category: Baker, H M.]]
[[Category: Mc Carthy AA]]
[[Category: Carthy, A A.Mc.]]
[[Category: Patchett ML]]
[[Category: Patchett, M L.]]
[[Category: Shewry SC]]
[[Category: Shewry, S C.]]
[[Category: Epimerisation]]
[[Category: Metal-assisted catalysis]]
[[Category: Methylmalonyl-coa]]
[[Category: Vicinal oxygen chelate superfamily]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 21:02:31 2008''

Latest revision as of 10:38, 7 February 2024

Crystal Structure of Native Methylmalonyl-CoA EpimeraseCrystal Structure of Native Methylmalonyl-CoA Epimerase

Structural highlights

1jc5 is a 6 chain structure with sequence from Propionibacterium freudenreichii subsp. shermanii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q8VQN0_PROFR

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1jc5, resolution 2.20Å

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OCA
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