Amino acid sequence and tertiary structure of Cratylia mollis seed lectin

Abstract

Carbohydrate-protein interactions play a key role in many biological processes. Cramoll is a lectin purified from Cratylia mollis seeds that is taxonomically related to concanavalin A (Con A). Although Cramoll and Con A have the same monosaccharide specificity, they have different glycoprotein binding profiles. We report the primary structure of Cramoll, determined by Edman degradation and mass spectrometry and its 1.77 A crystallographic structure and compare it with the three-dimensional structure of Con A in an attempt to understand how differential binding can be achieved by similar or nearly identical structures. We report here that Cramoll consists of 236 residues, with 82% identity with Con A, and that its topological architecture is essentially identical to Con A, because the Calpha positional differences are below 3.5 A. Cramoll and Con A have identical binding sites for MealphaMan, Mn2+, and Ca2+. However, we observed six substitutions in a groove adjacent to the extended binding site and two in the extended binding site that may explain the differences in binding of oligosaccharides and glycoproteins between Cramoll and Con A.

Impedimetric biosensor based on self-assembled hybrid cystein-gold nanoparticles and CramoLL lectin for bacterial lipopolysaccharide recognition

“…They demonstrate that this lectin retains its biological capability after exposition on the electrode surface. This behavior can be explained by the studies that were performed to determine the relevance of the neighborhoods of the monosaccharide-binding sites and accounts for the CramoLL response obtained for the bacterial LPS [20].…”

“…CramoLL has monosaccharide binding sites with hydrogen bond interactions between protein and methyl-a-D-mannoside (MeaMan). One molecule of MeaMan in the monosaccharide binding site interacts through direct hydrogen bonds with Asn14, Leu99, Tyr100, Asp207, and Arg227 and through hydrophobic contacts with the side chains of Tyr12, Leu99, and Tyr100 [20].…”

Determinación de la estructura primaria de la lectina V-2 de semillas de arveja (Pisum sativum L.) y su efecto antibacteriano en Staphylococcus aureus y Escherichia coli

“…La lectina Cramoll de C. mollis, con la cual la lectina V-2 de P. sativum tiene el más alto porcentaje de homología secuencial (91,4%), es una lectina de 236 residuos, con cuatro subunidades y capaz de unirse a metales como calcio y manganeso y a la glucosa/manosa (Souza et al, 2003).…”

<i>In Vitro</i> Evaluation of Gamma Irradiation on a Gel Formulation of Cratylia Mollis: Rheological Proporties and Microbiological Control

“…Molecular forms of the lectin from seeds of C. mollis (Cramoll 1, Cramoll 2, Cramoll 3 and Cramoll 4) have been extensively purified and characterized [6][7][8]. Cramoll 1, 2 and 4 are lectins that bind specifically to glucose/ mannose, while Cramoll 3 is a galactose-specific glycoprotein.…”

“…Cramoll 1, 2 and 4 are lectins that bind specifically to glucose/ mannose, while Cramoll 3 is a galactose-specific glycoprotein. Preparations containing isoforms (Cramoll-1,4) and isolectinas (Cramoll 1, 2, 3), as well as a Cramoll were structurally analyzed and used in various biotechnological applications [8][9][10][11][12][13][14][15][16].…”