4h2c

Trehalulose synthase MutB R284C mutant

spinqualitylabelsall models 4h2c, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4h2c is a 1 chain structure with sequence from Rhizobium sp. MX-45. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: CA, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function M1E1F6_9HYPH Publication Abstract from PubMed 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. Mutations inducing an active-site aperture in Rhizobium sp. sucrose isomerase confer hydrolytic activity.,Lipski A, Watzlawick H, Ravaud S, Robert X, Rhimi M, Haser R, Mattes R, Aghajari N Acta Crystallogr D Biol Crystallogr. 2013 Feb;69(Pt 2):298-307. doi:, 10.1107/S0907444912045532. Epub 2013 Jan 19. PMID:23385465 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Trehalulose synthase

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