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NMR assignments and ligand-binding studies on a two-domain family GH19 chitinase allergen from Japanese cedar (Cryptomeria japonica) pollen

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Abstract

A two-domain family GH19 chitinase from Japanese cedar (Cryptomeria japonica) pollen, CJP-4, which consists of an N-terminal CBM18 domain and a GH19 catalytic domain, is known to be an important allergen, that causes pollinosis. We report here the resonance assignments of the NMR spectrum of CJP-4. The backbone resonances were almost completely assigned, and the secondary structure was estimated based on the chemical shift values. The addition of a chitin dimer to the enzyme solution perturbed the chemical shifts of the resonances of amino acid residues forming a long extended binding site spanning from the CBM18 domain to the GH19 catalytic domain.

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Abbreviations

CJP-4:

A class IV chitinase allergen from Cryptomeria japonica

GlcNAc:

N-acetyl-d-glucosamine

(GlcNAc)n :

β-1,4-Linked oligosaccharide of GlcNAc

NMR:

Nuclear magnetic resonance

HSQC:

Two-dimensional heteronuclear single quantum correlation

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Funding

This work was supported by “Strategic Project to Support the Formation of Research Bases at Private Universities: Matching Fund Subsidy from MEXT (Ministry of Education, Culture, Sports, Science and Technology, Japan)”, 2011–2015 (S1101035), to TF.

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Authors and Affiliations

  1. Department of Advanced Bioscience, Kindai University, 3327-204, Nakamachi, Nara, 631-8505, Japan

    Tomoya Takashima, Takayuki Ohnuma & Tamo Fukamizo

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  1. Tomoya Takashima
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  2. Takayuki Ohnuma
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  3. Tamo Fukamizo
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Correspondence to Tamo Fukamizo.

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Takashima, T., Ohnuma, T. & Fukamizo, T. NMR assignments and ligand-binding studies on a two-domain family GH19 chitinase allergen from Japanese cedar (Cryptomeria japonica) pollen. Biomol NMR Assign 11, 85–90 (2017). https://doi.org/10.1007/s12104-016-9725-4

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  • DOI: https://doi.org/10.1007/s12104-016-9725-4

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