5YGM

Monomeric structure of concanavalin A at pH 7.5 from Carnivalia ensiformis

Summary for 5YGM

• Entry DOI: 10.2210/pdb5ygm/pdb
• Descriptor: Concanavalin-A, CALCIUM ION, MANGANESE (II) ION, ... (4 entities in total)
• Functional Keywords: concanavalin a, sugar binding protein
• Biological source: Canavalia ensiformis (Jack bean); More
• Total number of polymer chains: 1
• Total formula weight: 25717.40

Authors

Park, J.H.,Park, Y.R.,Lee, S.J. (deposition date: 2017-09-24, release date: 2017-10-25, Last modification date: 2023-11-22)

Primary citation

Chung, N.J.,Park, Y.R.,Lee, D.H.,Oh, S.Y.,Park, J.H.,Lee, S.J.
Heterometal-Coordinated Monomeric Concanavalin A at pH 7.5 from Canavalia ensiformis
J. Microbiol. Biotechnol., 27:2241-2244, 2017

PubMed Abstract: The structure of concanavalin A (ConA) has been studied intensively owing 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 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.

PubMed: 29025256
DOI: 10.4014/jmb.1709.09057

Experimental method

X-RAY DIFFRACTION (1.6 Å)