Literature DB >> 23908050

Crystallization and preliminary X-ray crystallographic analysis of cycloisomaltooligosaccharide glucanotransferase from Bacillus circulans T-3040.

Nobuhiro Suzuki1, Young Min Kim, Mitsuru Momma, Zui Fujimoto, Mikihiko Kobayashi, Atsuo Kimura, Kazumi Funane.   

Abstract

Bacillus circulans T-3040 cycloisomaltooligosaccharide glucanotransferase (BcCITase) catalyses an intramolecular transglucosylation reaction and produces cycloisomaltooligosaccharides from dextran. BcCITase was overexpressed in Escherichia coli in two different forms and crystallized by the sitting-drop vapour-diffusion method. The crystal of BcCITase bearing an N-terminal His₆ tag diffracted to a resolution of 2.3 Å and belonged to space group P3₁21, containing a single molecule in the asymmetric unit. The crystal of BcCITase bearing a C-terminal His6 tag diffracted to a resolution of 1.9 Å and belonged to space group P2₁2₁2₁, containing two molecules in the asymmetric unit.

Entities:  

Keywords:  Bacillus circulans; cycloisomaltooligosaccharide glucanotransferase; dextran; glycoside hydrolase family 66

Mesh:

Substances:

Year:  2013        PMID: 23908050      PMCID: PMC3729181          DOI: 10.1107/S174430911301991X

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


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1.  Structural elucidation of the cyclization mechanism of α-1,6-glucan by Bacillus circulans T-3040 cycloisomaltooligosaccharide glucanotransferase.

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