3vss | pdb_00003vss

Microbacterium saccharophilum K-1 beta-fructofuranosidase catalytic domain complexed with fructose

spinqualitylabelsall models 3vss, resolution 1.97Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3vss is a 1 chain structure with sequence from Microbacterium saccharophilum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.97Å Ligands: FRU Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8VW87_9MICO Publication Abstract from PubMed Arthrobacter sp. K-1 beta-fructofuranosidase (ArFFase), a glycoside hydrolase family 68 enzyme, catalyzes the hydrolysis and transfructosylation of sucrose. ArFFase is useful for producing a sweetener, lactosucrose (4(G)-beta-d-galactosylsucrose). The primary structure of ArFFase is homologous to those of levansucrases, although ArFFase catalyzes mostly hydrolysis when incubated with sucrose alone, even at high concentration. Here, we determined the crystal structure of ArFFase in unliganded form and complexed with fructose. ArFFase consisted of a five-bladed beta-propeller fold as observed in levansucrases. The structure of ArFFase was most similar to that of Gluconacetobacter diazotrophicus levansucrase (GdLev). The structure of the catalytic cleft of ArFFase was also highly homologous to that of GdLev. However, two amino acid residues, Tyr232 and Pro442 in ArFFase, were not conserved between them. A tunnel observed at the bottom of the catalytic cleft of ArFFase may serve as a water drain or its reservoir. Crystal structure of a lactosucrose-producing enzyme, Arthrobacter sp. K-1 beta-fructofuranosidase.,Tonozuka T, Tamaki A, Yokoi G, Miyazaki T, Ichikawa M, Nishikawa A, Ohta Y, Hidaka Y, Katayama K, Hatada Y, Ito T, Fujita K Enzyme Microb Technol. 2012 Dec 10;51(6-7):359-65. doi:, 10.1016/j.enzmictec.2012.08.004. Epub 2012 Aug 16. PMID:23040392 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA