Heterometal-Coordinated Monomeric Concanavalin A at pH 7.5 from Canavalia ensiformis
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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.
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.
참고문헌 (21)
- Kim D, "Exploration of the metal coordination region of concanavalin A for its interaction with human norovirus", Biomaterials, 128, pp.33~43 (2017)
- Balzarini J., "Targeting the glycans of glycoproteins: a novel paradigm for antiviral therapy", Nat. Rev. Microbiol, 5, pp.583~597 (2007)
- Bronzoni RV, "Detection of infectious bronchitis virus and specific anti-viral antibodies using a concanavalin Asandwich-ELISA", Viral Immunol, 18, pp.569~578 (2005)
- Garrison AR, "The cyanobacterial lectin scytovirin displays potent in vitro and in vivo activity against Zaire Ebola virus", Antiviral Res, 112, pp.1~7 (2014)
- O’Keefe BR, "Broad-sp ectrum in v itro a ctivity and in vivo efficacy of the antiviral protein griffithsin against emerging viruses of the family Coronaviridae", J. Virol, 84, pp.2511~2521 (2010)
- Okino CH, "Humoral and cell-mediated immune responses to different doses of attenuated vaccine against avian infectious bronchitis virus", Viral Immunol, 26, pp.259~267 (2013)
- Bouckaert J, "The structural features of concanavalin A governing nonproline peptide isomerization", J. Biol. Chem, 275, pp.19778~19787 (2000)
- Doyle R, "Lectins in diagnostic microbiology", Eur. J. Clin. Microbiol, 3, pp.4~9 (1984)
- Gerlits OO, "Mannobiose binding induces changes in hydrogen bonding and protonation states of acidic residues in concanavalin A as revealed by neutron crystallography", Biochemistry, 56, pp.4747~4750 (2017)
- Kadirvelraj R, "Involvement of water in carbohydrate-protein binding:concanavalin A revisited", J. Am. Chem. Soc, 130, pp.16933~16942 (2008)
- Bouckaert J, "Zinc", calcium- and cadmium, Acta Crystallogr. D Biol. Crystallogr, pp.2000, 56[DOI]
- Kantardjieff KA, "Concanavalin A in a dimeric crystal form: revisiting structural accuracy and molecular flexibility", Acta Crystallogr. D Biol. Crystallogr, 58, pp.735~743 (2002)
- Cao S, "Structural basis for the recognition of blood group trisaccharides by norovirus", J. Virol, 81, pp.5949~5957 (2007)
- Auer HE, "pH-dependent changes in properties of concanavalin A in the acid pH range", Int. J. Pept. Protein Res, 24, pp.462~471 (1984)
- -Man upon binding, "Glycobiology", 1998, 173~181
- Sinha S, "Unfolding studies on soybean agglutinin and concanavalin A tetramers: a comparative account", Biophys. J, 88, pp.1300~1310 (2005)
- Kaushik S, "The role of metal ions in substrate recognition and stability of concanavalin A: a molecular dynamics study", Biophys. J, 96, pp.21~34 (2009)
- Christie DJ, "Conformational changes following Mn(II) binding to demetalized concanavalin A1", Biochem. Biophys. Res. Commun, 95, pp.1043~1048 (1980)
- Pandolfino ER, "Location of Mn2+ in concanavalin A containing only a Mn2+ion", Biochem. Biophys. Res. Commun, 96, pp.1248~1252 (1980)
- Magnuson JA, "Metal ion binding to concanavalin A", J. Biosci, 5, pp.9~17 (1983)
- Bezerra GA, "Structural analysis of Canavalia maritima and Canavalia gladiata lectins complexed with different dimannosides: new insights into the understanding of the structure-biological activity relationship in legume lectins", J. Struct. Biol, 160, pp.168~176 (2007)
