Abstract
The structure of concanavalin A (ConA) has been studied intensively owing to its specific interactions with carbohydrates and its heterometal (Ca 2+ and Mn 2+ ) coordination. Most structures from X-ray crystallography have shown ConA as a dimer or tetramer, because the complex formation requires specific crystallization conditions. Here, we reported the monomeric structure of ConA with a resolution of 1.6 Å, which revealed that metal coordination could trigger sugar-binding ability. The calcium coordination residue, Asn14, changed the orientation of carbohydrate-binding residues and biophysical details, including structural information, providing valuable clues for the development and application of detection kits using ConA.
| Original language | English |
|---|---|
| Pages (from-to) | 2241-2244 |
| Number of pages | 4 |
| Journal | Journal of Microbiology and Biotechnology |
| Volume | 27 |
| Issue number | 12 |
| DOIs | |
| State | Published - 2017.12 |
Keywords
- Concanavalin A
- Heterometal coordination
- Lectins
- Microbial detection
- Sugar binding region
Quacquarelli Symonds(QS) Subject Topics
- Biological Sciences
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