1jc4: Difference between revisions
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|PDB= 1jc4 |SIZE=350|CAPTION= <scene name='initialview01'>1jc4</scene>, resolution 2.00Å | |PDB= 1jc4 |SIZE=350|CAPTION= <scene name='initialview01'>1jc4</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|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] | |ACTIVITY= <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> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1jc5|1JC5]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jc4 OCA], [http://www.ebi.ac.uk/pdbsum/1jc4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jc4 RCSB]</span> | |||
}} | }} | ||
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[[Category: Patchett, M L.]] | [[Category: Patchett, M L.]] | ||
[[Category: Shewry, S C.]] | [[Category: Shewry, S C.]] | ||
[[Category: methylmalonyl-coa]] | [[Category: methylmalonyl-coa]] | ||
[[Category: vicinal oxygen chelate superfamily]] | [[Category: vicinal oxygen chelate superfamily]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:31:30 2008'' | ||
Revision as of 21:31, 30 March 2008
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| , resolution 2.00Å | |||||||
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| Ligands: | , | ||||||
| Activity: | Methylmalonyl-CoA epimerase, with EC number 5.1.99.1 | ||||||
| Related: | 1JC5
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Se-Met Methylmalonyl-CoA Epimerase
OverviewOverview
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.
About this StructureAbout this Structure
1JC4 is a Single protein structure of sequence from Propionibacterium freudenreichii subsp. shermanii. Full crystallographic information is available from OCA.
ReferenceReference
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
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