4GI6
Crystal structure of the MUTB F164L mutant in complex with glucose
Summary for 4GI6
| Entry DOI | 10.2210/pdb4gi6/pdb |
| Related | 1ZJA 1ZJB 2PWD 2PWE 2PWF 2PWG 2PWH 4GI8 4GI9 4GIA 4GIN 4H2C |
| Descriptor | Sucrose isomerase, CALCIUM ION, alpha-D-glucopyranose, ... (6 entities in total) |
| Functional Keywords | enzyme complex, tim-barrel(beta/alpha)8, sucrose isomerase, glycoside hydrolase, trehalulose synthase, gh13 family(cazy database), calcium binding, isomerase |
| Biological source | Rhizobium |
| Total number of polymer chains | 2 |
| Total formula weight | 128928.87 |
| Authors | Lipski, A.,Haser, R.,Aghajari, N. (deposition date: 2012-08-08, release date: 2013-02-13, Last modification date: 2023-11-08) |
| Primary citation | Lipski, A.,Watzlawick, H.,Ravaud, S.,Robert, X.,Rhimi, M.,Haser, R.,Mattes, R.,Aghajari, N. Mutations inducing an active-site aperture in Rhizobium sp. sucrose isomerase confer hydrolytic activity Acta Crystallogr.,Sect.D, 69:298-307, 2013 Cited by PubMed Abstract: Sucrose isomerase is an enzyme that catalyzes the production of sucrose isomers of high biotechnological and pharmaceutical interest. Owing to the complexity of the chemical synthesis of these isomers, isomaltulose and trehalulose, enzymatic conversion remains the preferred method for obtaining these products. Depending on the microbial source, the ratio of the sucrose-isomer products varies significantly. In studies aimed at understanding and explaining the underlying molecular mechanisms of these reactions, mutations obtained using a random-mutagenesis approach displayed a major hydrolytic activity. Two of these variants, R284C and F164L, of sucrose isomerase from Rhizobium sp. were therefore crystallized and their crystal structures were determined. The three-dimensional structures of these mutants allowed the identification of the molecular determinants that favour hydrolytic activity compared with transferase activity. Substantial conformational changes resulting in an active-site opening were observed, as were changes in the pattern of water molecules bordering the active-site region. PubMed: 23385465DOI: 10.1107/S0907444912045532 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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