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ファイル
言語
英語
著者
Yorinaga, Yutaka Department of Life Science and Biotechnology, Faculty of Life and Environmental Science, Shimane University, 1060 Nishikawatsu, Matsue 690-8504, Japan
Kumasaka, Takashi Japan Synchrotron Radiation Research Institute (JASRI), Sayo, Hyogo 679-5198 Japan
Yamamoto, Masaki RIKEN SPring-8 Center, Sayo, Hyogo, 679-5148 Japan
Hamada, Kensaku X-ray Research Laboratory, Rigaku Co., Akishima, Tokyo, 196-8666 Japan
内容記述(抄録等)
Chitosanases belong to glycoside hydrolase families 5, 7, 8, 46, 75 and 80 and hydrolyse glucosamine polymers produced by partial or full deacetylation of chitin. Herein, we determined the crystal structure of chitosanase from the β‐proteobacterium, Mitsuaria chitosanitabida, (McChoA) at 1.75 Å resolution; the first structure of a family 80 chitosanase. McChoA is a 34 kDa extracellular protein of 301 amino acids that fold into two (upper and lower) globular domains with an active site cleft between them. Key substrate‐binding features are conserved with family 24 lysozymes and family 46 chitosanases. The distance between catalytic residues E41 and E61 (10.8 Å) indicates an inverting type mechanism. Uniquely, three disulphide bridges and the C terminus might contribute to enzyme activity.
主題
Chitosan
chitosanase
crystal structure
Mitsuaria
掲載誌名
FEBS Letters
591
3
開始ページ
540
終了ページ
547
ISSN(Online)
1873-3468
発行日
2017-1-13
DOI
出版者
the Federation of European Biochemical Societies
資料タイプ
学術雑誌論文
ファイル形式
PDF
著者版/出版社版
著者版
業績ID
e31384
部局
生物資源科学部
備考
This is the peer reviewed version of the following article: https://febs.onlinelibrary.wiley.com/doi/full/10.1002/1873-3468.12557, which has been published in final form at https://doi.org/10.1002/1873-3468.12557. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions.
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