Indexed by:期刊论文
Date of Publication:2018-01-01
Journal:ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
Included Journals:SCIE、PubMed
Volume:74
Issue:Pt 1
Page Number:30-40
ISSN No.:2059-7983
Key Words:chitin; chitinase; chitin synthesis; chitin degradation; synergy
Abstract:The glycoside hydrolase family 18 chitinases degrade or alter chitin. Multiple catalytic domains in a glycoside hydrolase family 18 chitinase function synergistically during chitin degradation. Here, an insect group III chitinase from the agricultural pest Ostrinia furnacalis (OfChtIII) is revealed to be an arthropod-conserved chitinase that contains two nonsynergistic GH18 domains according to its catalytic properties. Both GH18 domains are active towards single-chained chitin substrates, but are inactive towards insoluble chitin substrates. The crystal structures of each unbound GH18 domain, as well as of GH18 domains complexed with hexa-N-acetyl-chitohexaose or penta-N-acetyl-chitopentaose, suggest that the two GH18 domains possess endo-specific activities. Physiological data indicated that the developmental stage-dependent gene-expression pattern of OfChtIII was the same as that of the chitin synthase OfChsA but significantly different from that of the chitinase OfChtI, which is indispensable for cuticular chitin degradation. Additionally, immunological staining indicated that OfChtIII was co-localized with OfChsA. Thus, OfChtIII is most likely to be involved in the chitin-synthesis pathway.
Professor
Supervisor of Doctorate Candidates
Supervisor of Master's Candidates
Gender:Male
Alma Mater:Dalian University of Technology
Degree:Doctoral Degree
School/Department:School of Bioengineering
Discipline:Biochemical Engineering. Biochemistry and Molecular Biolog
Business Address:Room 445, School of Bioengineering
Contact Information:tianliu@dlut.edu.cn
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