4GG1
Crystal Structure of Benzoylformate Decarboxylase Mutant L403T
Summary for 4GG1
| Entry DOI | 10.2210/pdb4gg1/pdb |
| Descriptor | Benzoylformate decarboxylase, 2-{3-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-4-METHYL-2-OXO-2,3-DIHYDRO-1,3-THIAZOL-5-YL}ETHYL TRIHYDROGEN DIPHOSPHATE, CALCIUM ION, ... (6 entities in total) |
| Functional Keywords | decarboxylase, thiamin diphosphate cofactor, thiamin thiazolone diphosphate, lyase |
| Biological source | Pseudomonas putida |
| Total number of polymer chains | 1 |
| Total formula weight | 58191.50 |
| Authors | Novak, W.R.P.,Andrews, F.H.,Tom, A.R.,Gunderman, P.R.,McLeish, M.J. (deposition date: 2012-08-04, release date: 2013-05-22, Last modification date: 2023-09-13) |
| Primary citation | Andrews, F.H.,Tom, A.R.,Gunderman, P.R.,Novak, W.R.,McLeish, M.J. A bulky hydrophobic residue is not required to maintain the v-conformation of enzyme-bound thiamin diphosphate. Biochemistry, 52:3028-3030, 2013 Cited by PubMed Abstract: It is widely accepted that, in thiamin diphosphate (ThDP)-dependent enzymes, much of the rate acceleration is provided by the cofactor. Inter alia, the reactive conformation of ThDP, known as the V-conformation, has been attributed to the presence of a bulky hydrophobic residue located directly below the cofactor. Here we report the use of site-saturation mutagenesis to generate variants of this residue (Leu403) in benzoylformate decarboxylase. The observed 3 orders of magnitude range in k(cat)/K(m) values suggested that conformational changes in the cofactor could be influencing catalysis. However, X-ray structures of several variants were determined, and there was remarkably little change in ThDP conformation. Rather, it seemed that, once the V-conformation was attained, residue size and hydrophobicity were more important for enzyme activity. PubMed: 23607689DOI: 10.1021/bi400368j PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.069 Å) |
Structure validation
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