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Glycobiology Advance Access originally published online on September 9, 2003
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Glycobiology, 2003, Vol. 13, No. 12 961-972
© 2003 Oxford University Press

Amino acid sequence and tertiary structure of Cratylia mollis seed lectin

Gustavo A. de Souza2, Paulo S.L. Oliveira3,4, Stefano Trapani3, Ana Célia O. Santos5, José C. Rosa2, Helen J. Laure2, Vitor M. Faça2, Maria T.S. Correia6, Gisele A. Tavares3,4, Glaucius Oliva3, Luana C.B.B. Coelho6 and Lewis J. Greene1,2

2 Centro de Quimica de Proteínas and Depto de Biologia Celular, Molecular e Bioagentes Patogênicos, Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo, 14049-900 Ribeirão Preto, SP, Brazil; 3 Instituto de Física de São Carlos, Universidade de São Paulo, 13560-970, São Carlos, SP, Brazil; 4 Instituto de Química de São Carlos, Universidade de São Paulo, 13560-970, São Carlos, SP, Brazil; 5 Departamento de Ciências Fisiológicas, Instituto de Ciências Biológicas, Universidade de Pernambuco, Recife, PE, Brazil, and 6 Departamento de Bioquímica, Centro de Ciências Biológicas, Universidade Federal de Pernambuco, Recif, PE, Brazil

Received on August 6, 2003; revised on August 25, 2003; accepted on August 26, 2003

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 Å 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 C{alpha} positional differences are below 3.5 Å. Cramoll and Con A have identical binding sites for Me{alpha}Man, 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.

1 To whom correspondence should be addressed; e-mail: ljgreene{at}fmrp.usp.br


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