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FEBS Lett. 2017 Feb;591(3):540-547. doi: 10.1002/1873-3468.12557. Epub 2017 Jan 29.

Crystal structure of a family 80 chitosanase from Mitsuaria chitosanitabida.

Author information

1
Department of Life Science and Biotechnology, Faculty of Life and Environmental Science, Shimane University, Matsue, Japan.
2
Japan Synchrotron Radiation Research Institute (JASRI), Sayo, Hyogo, Japan.
3
RIKEN SPring-8 Center, Sayo, Hyogo, Japan.
4
X-ray Research Laboratory, Rigaku Co., Akishima, Tokyo, Japan.

Abstract

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.

KEYWORDS:

Mitsuaria ; chitosan; chitosanase; crystal structure

PMID:
28084023
DOI:
10.1002/1873-3468.12557
[Indexed for MEDLINE]
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