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language
eng
Author
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
Description
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.
Subject
Chitosan
chitosanase
crystal structure
Mitsuaria
Journal Title
FEBS Letters
Volume
591
Issue
3
Start Page
540
End Page
547
ISSN(Online)
1873-3468
Published Date
2017-1-13
DOI
Publisher
the Federation of European Biochemical Societies
NII Type
Journal Article
Format
PDF
Text Version
著者版
Gyoseki ID
e31384
OAI-PMH Set
Faculty of Life and Environmental Science
Remark
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.