Related Experiment Video
Updated: Jan 11, 2026

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
Published on: October 2, 2017
Functional and Structural Determination of a CBM101 Family Carbohydrate-Binding Module (CBM): A Single Residue Change
Xuanwei Mei1,2, Menghui Sun1, Guanchen Liu3
1State Key Laboratory of Marine Food Processing & Safety Control, College of Food Science and Engineering, Ocean University of China, 1299 Sansha Road, Qingdao 266404, China.
Abstract:
Carbohydrate-binding modules (CBMs) make up a class of protein domains that are favorable tools for the studies and applications of carbohydrates. Agarose and funoran are galactans derived from red algae with structural similarities and subtle differences. The CBM101 family was established following the discovery of WfCBM101, which showed a binding capacity to agarose. Herein, we performed functional and structural analyses of WfCBM101. The results showed that WfCBM101 binds to funoran, which represents the first identified funoran-binding CBM. The structure of WfCBM101 was resolved at a 1.5 Å resolution by X-ray crystallography. The protein displays a β-sandwich fold with two antiparallel β-sheets composed of 7 β-strands. Mutagenesis studies revealed an unusual phenomenon in which the mutation of a single residue K96 reshapes the protein specificity. These findings highlight the fine-tuned recognition and binding capacities of CBMs, and they may facilitate the future discovery of carbohydrate-binding proteins.
Related Concept Videos
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
Gene Families
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
Conserved Binding Sites
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
Ligand Binding and Linkage
Structure of Cadherins
Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...

