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Structure paper

TitleConformational changes on substrate binding to methylmalonyl CoA mutase and new insights into the free radical mechanism.
Journal, issue, pagesStructure, Vol. 6, Page 711-720, Year 1998
Publish dateSep 22, 1997 (structure data deposition date)
AuthorsMancia, F. / Evans, P.R.
External linksStructure / PubMed:9655823
MethodsX-ray diffraction
Resolution2.2 - 2.7 Å
Structure data

PDB-2req:
METHYLMALONYL-COA MUTASE, NON-PRODUCTIVE COA COMPLEX, IN OPEN CONFORMATION REPRESENTING SUBSTRATE-FREE STATE
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-3req:
METHYLMALONYL-COA MUTASE, SUBSTRATE-FREE STATE (POOR QUALITY STRUCTURE)
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-4req:
Methylmalonyl-COA Mutase substrate complex
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-COA:
COENZYME A

ChemComp-B12:
COBALAMIN

ChemComp-HOH:
WATER

ChemComp-ADN:
ADENOSINE

ChemComp-SCA:
SUCCINYL-COENZYME A

ChemComp-MCA:
METHYLMALONYL-COENZYME A

ChemComp-5AD:
5'-DEOXYADENOSINE

ChemComp-GOL:
GLYCEROL

Source
  • propionibacterium freudenreichii subsp. shermanii (bacteria)
KeywordsISOMERASE / MUTASE / INTRAMOLECULAR TRANSFERASE / COMPLEX (ISOMERASE/DEOXYADENOSINE) / COMPLEX (ISOMERASE-DEOXYADENOSINE) / COMPLEX (ISOMERASE-DEOXYADENOSINE) complex

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