Structure of a consensus chitin-binding domain revealed by solution NMR
Chitin-binding proteins (CBPs) are a versatile group of proteins found in almost every organism on earth. CBPs are involved in enzymatic carbohydrate degradation and also serve as templating scaffolds in the exoskeleton of crustaceans and insects. One specific chitin-binding motif found across a wid...
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Format: | Journal Article |
Language: | English |
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2022
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Online Access: | https://hdl.handle.net/10356/160526 |
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author | Heymann, Dario Mohanram, Harini Kumar, Akshita Verma, Chandra Shekhar Lescar, Julien Miserez, Ali |
author2 | School of Materials Science and Engineering |
author_facet | School of Materials Science and Engineering Heymann, Dario Mohanram, Harini Kumar, Akshita Verma, Chandra Shekhar Lescar, Julien Miserez, Ali |
author_sort | Heymann, Dario |
collection | NTU |
description | Chitin-binding proteins (CBPs) are a versatile group of proteins found in almost every organism on earth. CBPs are involved in enzymatic carbohydrate degradation and also serve as templating scaffolds in the exoskeleton of crustaceans and insects. One specific chitin-binding motif found across a wide range of arthropods' exoskeletons is the "extended Rebers and Riddiford" consensus (R&R), whose mechanism of chitin binding remains unclear. Here, we report the 3D structure and molecular level interactions of a chitin-binding domain (CBD-γ) located in a CBP from the beak of the jumbo squid Dosidicus gigas. This CBP is one of four chitin-binding proteins identified in the beak mouthpart of D. gigas and is believed to interact with chitin to form a scaffold network that is infiltrated with a second set of structural proteins during beak maturation. We used solution state NMR spectroscopy to elucidate the molecular interactions between CBD-γ and the soluble chitin derivative pentaacetyl-chitopentaose (PCP), and find that folding of CBD-γ is triggered upon its interaction with PCP. To our knowledge, this is the first experimental 3D structure of a CBP containing the R&R consensus motif, which can be used as a template to understand in more details the role of the R&R motif found in a wide range of CBP-chitin complexes. The present structure also provides molecular information for biomimetic synthesis of graded biomaterials using aqueous-based chemistry and biopolymers. |
first_indexed | 2024-10-01T06:09:59Z |
format | Journal Article |
id | ntu-10356/160526 |
institution | Nanyang Technological University |
language | English |
last_indexed | 2024-10-01T06:09:59Z |
publishDate | 2022 |
record_format | dspace |
spelling | ntu-10356/1605262022-07-26T05:35:44Z Structure of a consensus chitin-binding domain revealed by solution NMR Heymann, Dario Mohanram, Harini Kumar, Akshita Verma, Chandra Shekhar Lescar, Julien Miserez, Ali School of Materials Science and Engineering School of Biological Sciences Bioinformatics Institute, A*STAR Biological & Biomimetic Material Laboratory @ NTU Center for Sustainable Materials NTU Institute of Structural Biology Science::Biological sciences Chitin Binding Domain Squid Beak Proteins Chitin-binding proteins (CBPs) are a versatile group of proteins found in almost every organism on earth. CBPs are involved in enzymatic carbohydrate degradation and also serve as templating scaffolds in the exoskeleton of crustaceans and insects. One specific chitin-binding motif found across a wide range of arthropods' exoskeletons is the "extended Rebers and Riddiford" consensus (R&R), whose mechanism of chitin binding remains unclear. Here, we report the 3D structure and molecular level interactions of a chitin-binding domain (CBD-γ) located in a CBP from the beak of the jumbo squid Dosidicus gigas. This CBP is one of four chitin-binding proteins identified in the beak mouthpart of D. gigas and is believed to interact with chitin to form a scaffold network that is infiltrated with a second set of structural proteins during beak maturation. We used solution state NMR spectroscopy to elucidate the molecular interactions between CBD-γ and the soluble chitin derivative pentaacetyl-chitopentaose (PCP), and find that folding of CBD-γ is triggered upon its interaction with PCP. To our knowledge, this is the first experimental 3D structure of a CBP containing the R&R consensus motif, which can be used as a template to understand in more details the role of the R&R motif found in a wide range of CBP-chitin complexes. The present structure also provides molecular information for biomimetic synthesis of graded biomaterials using aqueous-based chemistry and biopolymers. Ministry of Education (MOE) This research was funded by the Singapore Ministry of EducationMOE) through an Academic Research Fund (AcRF) Tier 2 grant (Grant MOE2015-T2-1-062). We also acknowledge financial support from the US Office of Naval Research -Global (ONR-G), grant no. N62909-17-12045. 2022-07-26T05:35:44Z 2022-07-26T05:35:44Z 2021 Journal Article Heymann, D., Mohanram, H., Kumar, A., Verma, C. S., Lescar, J. & Miserez, A. (2021). Structure of a consensus chitin-binding domain revealed by solution NMR. Journal of Structural Biology, 213(2), 107725-. https://dx.doi.org/10.1016/j.jsb.2021.107725 1047-8477 https://hdl.handle.net/10356/160526 10.1016/j.jsb.2021.107725 33744410 2-s2.0-85103798231 2 213 107725 en MOE2015-T2-1-062 Journal of Structural Biology © 2021 Elsevier Inc. All rights reserved. |
spellingShingle | Science::Biological sciences Chitin Binding Domain Squid Beak Proteins Heymann, Dario Mohanram, Harini Kumar, Akshita Verma, Chandra Shekhar Lescar, Julien Miserez, Ali Structure of a consensus chitin-binding domain revealed by solution NMR |
title | Structure of a consensus chitin-binding domain revealed by solution NMR |
title_full | Structure of a consensus chitin-binding domain revealed by solution NMR |
title_fullStr | Structure of a consensus chitin-binding domain revealed by solution NMR |
title_full_unstemmed | Structure of a consensus chitin-binding domain revealed by solution NMR |
title_short | Structure of a consensus chitin-binding domain revealed by solution NMR |
title_sort | structure of a consensus chitin binding domain revealed by solution nmr |
topic | Science::Biological sciences Chitin Binding Domain Squid Beak Proteins |
url | https://hdl.handle.net/10356/160526 |
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