Heterometal-coordinated monomeric concanavalin A at pH 7.5 from Canavalia ensiformis.


The structure of concanavalin A (ConA) has been studied intensively due to its specific interactions with carbohydrates and its heterometal (Ca2+ and Mn2+) 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 a 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, changes 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.

DOI: 10.4014/jmb.1709.09057

Cite this paper

@article{Chung2017HeterometalcoordinatedMC, title={Heterometal-coordinated monomeric concanavalin A at pH 7.5 from Canavalia ensiformis.}, author={Nam-Jin Chung and Yeo Reum Park and D Lee and Jung Hee Park and Seung Jae Lee}, journal={Journal of microbiology and biotechnology}, year={2017} }