8JIY

A carbohydrate binding domain of a putative chondroitinase

Summary for 8JIY

• Entry DOI: 10.2210/pdb8jiy/pdb
• Descriptor: DUF4955 domain-containing protein (2 entities in total)
• Functional Keywords: carbohydrate binding, sugar binding protein
• Biological source: Polaribacter haliotis
• Total number of polymer chains: 1
• Total formula weight: 27117.34

Authors

Liu, G.C.,Chang, Y.G. (deposition date: 2023-05-29, release date: 2023-09-20, Last modification date: 2024-04-03)

Primary citation

Liu, G.,Chang, Y.,Mei, X.,Chen, G.,Zhang, Y.,Jiang, X.,Tao, W.,Xue, C.
Identification and structural characterization of a novel chondroitin sulfate-specific carbohydrate-binding module: The first member of a new family, CBM100.
Int.J.Biol.Macromol., 255:127959-127959, 2024

PubMed Abstract: Chondroitin sulfate is a biologically and commercially important polysaccharide with a variety of applications. Carbohydrate-binding module (CBM) is an important class of carbohydrate-binding protein, which could be utilized as a promising tool for the applications of polysaccharides. In the present study, an unknown function domain was explored from a putative chondroitin sulfate lyase in PL29 family. Recombinant PhCBM100 demonstrated binding capacity to chondroitin sulfates with K values of 2.1 ± 0.2 × 10 M and 6.0 ± 0.1 × 10 M to chondroitin sulfate A and chondroitin sulfate C, respectively. The 1.55 Å resolution X-ray crystal structure of PhCBM100 exhibited a β-sandwich fold formed by two antiparallel β-sheets. A binding groove in PhCBM100 interacting with chondroitin sulfate was subsequently identified, and the potential of PhCBM100 for visualization of chondroitin sulfate was evaluated. PhCBM100 is the first characterized chondroitin sulfate-specific CBM. The novelty of PhCBM100 proposed a new CBM family of CBM100.

PubMed: 37951443
DOI: 10.1016/j.ijbiomac.2023.127959

Experimental method

X-RAY DIFFRACTION (1.55 Å)