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Okamura, Masachika*; Hase, Yoshihiro; Onishi, Noboru*; Narumi, Issei; Tanaka, Atsushi
JAEA-Review 2011-043, JAEA Takasaki Annual Report 2010, P. 105, 2012/01
Okazaki, Nobuo; Tamada, Taro; Kato, Masaru*; Miura, Yutaka*; Kobayashi, Kazuo*; Kuroki, Ryota
no journal, ,
We successed crystallization of glycosyltransferase (GTSase) from Sulfolobus shibatae DSM5389, and determined crystal structure with data which was collected at SPring-8 BL41XU. The enzyme has 729 amino acids and five domains. Domain A is major domain which has (
/
)8 barrel catalytic domain as in the usual alpha-amylase family enzymes. The catalytic center is located in the center of the (/)8 barrel. In the near (/)8 barrel, electric density of Mg
ion is observed. Some hydrogen bonding network is observed, too.
Okazaki, Nobuo; Tamada, Taro; Miura, Yutaka*; Feese, M. D.*; Kato, Masaru*; Komeda, Toshihiro*; Takehara, Kyoko*; Kobayashi, Kazuo*; Kondo, Keiji*; Kuroki, Ryota
no journal, ,
The crystal structure of glycosyltrehalose synthase (GTSase) from the hyperthermophilic archaeum Sulfolobus shibatae DSM5389 has been determined to 2.3 A resolution by X-ray crystallography. GTSase converts the glucosidic bond between the last two glucose residues of amylose from an alpha-1,4 bond to an alpha-1,1 bond, making a non-reducing glycosyl trehaloside in the first step of the biosynthesis of trehalose. The structure of GTSase can be divided into five domains. The central domain has the (beta/alpha)8 barrel fold which is conserved in the alpha-amylase family as the catalytic domain. Three invariant catalytic carboxylic amino acids in the alpha-amylase family are also found in GTSase at positions Asp241, Glu269 and Asp460 in the (beta/alpha)8 domain. Our previous study with KM1-GTSase has been shown that the maltooligosaccharides are converted to glycosyltrehalose by an intramolecular transglycosylation mechanism.
