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7BWO

Consensus chitin binding protein

Summary for 7BWO
Entry DOI10.2210/pdb7bwo/pdb
DescriptorChitin binding beak protein 3 (1 entity in total)
Functional Keywordschitin binding protein, cbp-gamma, suckerin chitin binding protein, rr consensus, sugar binding protein
Biological sourceDosidicus gigas (Humboldt squid)
Total number of polymer chains1
Total formula weight7058.85
Authors
Mohanram, H.,Miserez, A. (deposition date: 2020-04-15, release date: 2021-04-14, Last modification date: 2024-05-15)
Primary citationHeymann, D.,Mohanram, H.,Kumar, A.,Verma, C.S.,Lescar, J.,Miserez, A.
Structure of a consensus chitin-binding domain revealed by solution NMR.
J.Struct.Biol., 213:107725-107725, 2021
Cited by
PubMed Abstract: 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.
PubMed: 33744410
DOI: 10.1016/j.jsb.2021.107725
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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