7REQ
METHYLMALONYL-COA MUTASE, 2-CARBOXYPROPYL-COA INHIBITOR COMPLEX
Summary for 7REQ
| Entry DOI | 10.2210/pdb7req/pdb |
| Descriptor | PROTEIN (METHYLMALONYL-COA MUTASE), 2-CARBOXYPROPYL-COENZYME A, COBALAMIN, ... (6 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 | 303872.41 |
| Authors | Evans, P.R.,Mancia, F. (deposition date: 1998-09-10, release date: 1998-09-16, Last modification date: 2023-09-20) |
| Primary citation | Mancia, F.,Smith, G.A.,Evans, P.R. Crystal structure of substrate complexes of methylmalonyl-CoA mutase. Biochemistry, 38:7999-8005, 1999 Cited by PubMed Abstract: X-ray crystal structures of methylmalonyl-CoA mutase in complexes with substrate methylmalonyl-CoA and inhibitors 2-carboxypropyl-CoA and 3-carboxypropyl-CoA (substrate and product analogues) show that the enzyme-substrate interactions change little during the course of the rearrangement reaction, in contrast to the large conformational change on substrate binding. The substrate complex shows a 5'-deoxyadenine molecule in the active site, bound weakly and not attached to the cobalt atom of coenzyme B12, rotated and shifted from its position in the substrate-free adenosylcobalamin complex. The position of Tyralpha89 close to the substrate explains the stereochemical selectivity of the enzyme for (2R)-methylmalonyl-CoA. PubMed: 10387043DOI: 10.1021/bi9903852 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
Download full validation report
