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Crystal structure of glycosyltrehalose synthase from Sulfolobus shibatae DSM5389
https://repo.qst.go.jp/records/49278
https://repo.qst.go.jp/records/49278d86158b7-1887-4ebd-9bcf-9c1c0f47ee7b
| Item type | 学術雑誌論文 / Journal Article(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2018-11-27 | |||||
| タイトル | ||||||
| タイトル | Crystal structure of glycosyltrehalose synthase from Sulfolobus shibatae DSM5389 | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
| 資源タイプ | journal article | |||||
| アクセス権 | ||||||
| アクセス権 | metadata only access | |||||
| アクセス権URI | http://purl.org/coar/access_right/c_14cb | |||||
| 著者 |
岡崎, 伸生
× 岡崎, 伸生× Blaber, Michael× 黒木, 良太× 玉田, 太郎× 玉田 太郎 |
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| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | AbstractGlycosyltrehalose synthase (GTSase) converts the glucosidic bond between the last two glucose residues of amylose from an α-1,4 bond to an α-1,1 bond making a non-reducing glycosyl trehaloside in the first step of the biosynthesis of trehalose. To better understand the structural basis of the catalytic mechanism, the crystal structure of GTSase (5389-GTSase) from the hyperthermophilic archaeum Sulfolobus shibatae DSM5389 has been determined to 2.4 Å resolution by X-ray crystallography. The structure of 5389-GTSase can be divided into five domains. The central domain has the (β/α)8 barrel fold which is conserved in the α-amylase family as the catalytic domain. Three invariant catalytic carboxylic amino acids in the α-amylase family are also found in GTSase at positions Asp241, Glu269 and Asp460 in the catalytic domain. The shape of catalytic cavity and the pocket size at bottom of cavity correspond to the intramolecular transglycosylation mechanism proposed from previous enzymatic studies. | |||||
| 書誌情報 |
Acta Crystallographica Section F 巻 74, p. 741-746, 発行日 2018-11 |
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| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 2053-230X | |||||
| DOI | ||||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | 10.1107/S2053230X1801453X | |||||
