Chitin oligosaccharide binding to the lysin motif of a novel type of chitinase from the multicellular green alga, Volvox carteri

Chitin oligosaccharide binding to the lysin motif of a novel type of chitinase from the... Plant Mol Biol (2017) 93:97–108 DOI 10.1007/s11103-016-0549-5 Chitin oligosaccharide binding to the lysin motif of a novel type of chitinase from the multicellular green alga, Volvox carteri 1 1 2 1 Yoshihito Kitaoku  · Tamo Fukamizo  · Tomoyuki Numata  · Takayuki Ohnuma   Received: 27 July 2016 / Accepted: 30 September 2016 / Published online: 2 November 2016 © Springer Science+Business Media Dordrecht 2016 1 15 Abstract completely assign the main chain resonances of the H, N- Key message The chitinase-mediated defense sys- HSQC spectrum in a sequential manner. NMR-based titra- tem in higher plants has been intensively studied from tion experiments of chitin oligosaccharides, (GlcNAc) physiological and structural viewpoints. However, the (n = 3–6), revealed the ligand-binding site of VcLysM2, in defense system in the most primitive plant species, such which the Trp96 side chain appeared to interact with the as green algae, has not yet been elucidated in details. terminal GlcNAc residue of the ligand. We then mutated In this study, we solved the crystal structure of a fam- Trp96 to alanine (VcLysM2-W96A), and the mutant pro- ily CBM-50 LysM module attached to the N-terminus of tein was characterized. Based on isothermal titration chitinase from Volvox carteri, and successfully analyzed calorimetry, the affinity of (GlcNAc) toward VcLysM2 its http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Molecular Biology Springer Journals

Chitin oligosaccharide binding to the lysin motif of a novel type of chitinase from the multicellular green alga, Volvox carteri

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Publisher
Springer Netherlands
Copyright
Copyright © 2016 by Springer Science+Business Media Dordrecht
Subject
Life Sciences; Plant Sciences; Biochemistry, general; Plant Pathology
ISSN
0167-4412
eISSN
1573-5028
D.O.I.
10.1007/s11103-016-0549-5
Publisher site
See Article on Publisher Site

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