2REQ

METHYLMALONYL-COA MUTASE, NON-PRODUCTIVE COA COMPLEX, IN OPEN CONFORMATION REPRESENTING SUBSTRATE-FREE STATE

Summary for 2REQ

• Entry DOI: 10.2210/pdb2req/pdb
• Descriptor: METHYLMALONYL-COA MUTASE, COENZYME A, COBALAMIN, ... (5 entities in total)
• Functional Keywords: isomerase, mutase, intramolecular transferase
• Biological source: Propionibacterium freudenreichii subsp. shermanii; More
• Total number of polymer chains: 4
• Total formula weight: 303331.86

Authors

Evans, P.R.,Mancia, F. (deposition date: 1997-09-22, release date: 1998-01-28, Last modification date: 2024-05-22)

Primary citation

Mancia, F.,Evans, P.R.
Conformational changes on substrate binding to methylmalonyl CoA mutase and new insights into the free radical mechanism.
Structure, 6:711-720, 1998

PubMed Abstract: Methylmalonyl CoA mutase catalyses the interconversion of succinyl CoA and methylmalonyl CoA via a free radical mechanism. The enzyme belongs to a family of enzymes that catalyse intramolecular rearrangement reactions in which a group and a hydrogen atom on adjacent carbons are exchanged. These enzymes use the cofactor adenosylcobalamin (coenzyme B12) which breaks to form an adenosyl radical, thus initiating the reaction. Determination of the structure of substrate-free methylmalonyl CoA mutase was initiated to provide further insight into the mechanism of radical formation.

PubMed: 9655823
DOI: 10.1016/S0969-2126(98)00073-2

Experimental method

X-RAY DIFFRACTION (2.5 Å)