5ygm

Publication Abstract from PubMed

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 A, 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.

Heterometal-coordinated monomeric concanavalin A at pH 7.5 from Canavalia ensiformis.,Chung NJ, Park YR, Lee DH, Park JH, Lee SJ J Microbiol Biotechnol. 2017 Oct 13. doi: 10.4014/jmb.1709.09057. PMID:29025256^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.