Expression, crystallization and preliminary X-ray crystallographic analysis of cellobiose 2-epimerase from Dictyoglomus turgidum DSM 6724.

ABSTRACT: Cellobiose 2-epimerase epimerizes and isomerizes ?-1,4- and ?-1,4-gluco-oligosaccharides. N-Acyl-D-glucosamine 2-epimerase (DT_epimerase) from Dictyoglomus turgidum has an unusually high catalytic activity towards its substrate cellobiose. DT_epimerase was expressed, purified and crystallized. Crystals were obtained of both His-tagged DT_epimerase and untagged DT_epimerase. The crystals of His-tagged DT_epimerase diffracted to 2.6?Å resolution and belonged to the monoclinic space group P2?, with unit-cell parameters a=63.9, b=85.1, c=79.8?Å, ?=110.8°. With a Matthews coefficient VM of 2.18?Å3?Da(-1), two protomers were expected to be present in the asymmetric unit with a solvent content of 43.74%. The crystals of untagged DT_epimerase diffracted to 1.85?Å resolution and belonged to the orthorhombic space group P2?2?2?, with unit-cell parameters a=55.9, b=80.0, c=93.7?Å. One protomer in the asymmetric unit was expected, with a corresponding VM of 2.26?Å3?Da(-1) and a solvent content of 45.6%.

SUBMITTER: Pham TV 

PROVIDER: S-EPMC3792681 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature