The crystal structure of the chitinase ChiA74 of Bacillus thuringiensis has a multidomain assembly

Juárez-Hernández, Estefania O.; Casados-Vázquez, Luz E.; Brieba, Luis G.; Torres-Larios, Alfredo; Jimenez-Sandoval, Pedro; Barboza-Corona, José E.

doi:10.1038/s41598-019-39464-z

Title: The crystal structure of the chitinase ChiA74 of Bacillus thuringiensis has a multidomain assembly

Journal Article · 21 February 2019 · Scientific Reports

DOI: https://doi.org/10.1038/s41598-019-39464-z · OSTI ID:1544878

Juárez-Hernández, Estefania O. ^[1]; Casados-Vázquez, Luz E. ^[1]; Brieba, Luis G. ^[2]; Torres-Larios, Alfredo ^[3]; Jimenez-Sandoval, Pedro ^[2];

^[1]

Univ. de Guanajuato Campus Irapuato-Salamanca (México)
Inst. Politécnico Nacional, Irapuato, Guanajuato (México)
Univ. Nacional Autónoma de México, Ciudad de México (México)

There is no structural information about any chitinase synthesized by Bacillus thuringiensis, the most successful microbial insect larvicide used worldwide. In this study, we solved the 3D structure of the chitinase ChiA74 at 2.26 Å. The crystal structure shows that ChiA74 is composed of a modular arrangement formed by (i) a catalytic region (CD), (ii) a chitinase insertion domain (CID), (iii) a fibronectin type III domain (FnIII), and (iv) a chitin binding domain (CBD). The location of the CBD with respect to the CD has no structural similarity to other chitinases with known structures. The activity of a ChiA74 lacking its secretion signal peptide (ChiA74Δsp) and a truncated version lacking its CBD/FnIII domains (ChiA74Δsp-50) did not have statistical differences in activity against colloidal chitin. However, ChiA74Δsp exhibits 4.5 and 2.0 higher activity than versions lacking the CBD (ChiA74Δsp-60) and CBD/FnIII domains (ChiA74Δsp-50), respectively, when crystalline chitin was used as substrate. Our data suggest that the CBD might plays a significant role in crystalline chitin hydrolysis. We also demonstrated the importance of the catalytic E211 in the CD, as mutants ChiA74Δsp_E211N and ChiA74Δsp_{D207N, E211N} were inactive against colloidal and crystalline chitins, chitosan and 4-MU-GlcNAc₃. ChiA74 has a processive activity producing oligosaccharides with degree of polymerization (DP) of 1 (GlcNAc) and 2 (GlcNAc₂).

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22); Secretaría de Educación Pública-Consejo Nacional de Ciencia y Tecnología (SEP-CONACYT); Fronteras de la Ciencia-CONACYT; Cátedras-CONACYT; Michigan Economic Development Corporation and the Michigan Technology Tri-Corridor

Grant/Contract Number:: AC02-06CH11357

OSTI ID:: 1544878

Journal Information:: Scientific Reports, Journal Name: Scientific Reports Journal Issue: 1 Vol. 9; ISSN 2045-2322

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Matthews coefficient probabilities: Improved estimates for unit cell contents of proteins, DNA, and protein-nucleic acid complex crystals Kantardjieff, Katherine A.; Rupp, Bernhard Protein Science, Vol. 12, Issue 9 https://doi.org/10.1110/ps.0350503	journal	September 2003
The chitinolytic machinery of Serratia marcescens - a model system for enzymatic degradation of recalcitrant polysaccharides Vaaje-Kolstad, Gustav; Horn, Svein J.; Sørlie, Morten FEBS Journal, Vol. 280, Issue 13 https://doi.org/10.1111/febs.12181	journal	March 2013
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Microbial chitinases: properties, current state and biotechnological applications Le, Bao; Yang, Seung Hwan World Journal of Microbiology and Biotechnology, Vol. 35, Issue 9 https://doi.org/10.1007/s11274-019-2721-y	journal	September 2019
Chitinases of Bacillus thuringiensis: Phylogeny, Modular Structure, and Applied Potentials Martínez-Zavala, Sheila A.; Barboza-Pérez, Uriel E.; Hernández-Guzmán, Gustavo Frontiers in Microbiology, Vol. 10 https://doi.org/10.3389/fmicb.2019.03032	journal	January 2020

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Title: The crystal structure of the chitinase ChiA74 of Bacillus thuringiensis has a multidomain assembly

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