Artículos de revistas
Cdna Cloning And 1.75 Å Crystal Structure Determination Of Ppl2, An Endochitinase And N-acetylglucosamine-binding Hemagglutinin From Parkia Platycephala Seeds
Registro en:
Febs Journal. , v. 273, n. 17, p. 3962 - 3974, 2006.
1742464X
10.1111/j.1742-4658.2006.05400.x
2-s2.0-33747413686
Autor
Cavada B.S.
Moreno F.B.B.
Da Rocha B.A.M.
De Azevedo Jr. W.F.
Castellon R.E.R.
Goersch G.V.
Nagano C.S.
De Souza E.P.
Nascimento K.S.
Radis-Baptista G.
Delatorre P.
Leroy Y.
Toyama M.H.
Pinto V.P.T.
Sampaio A.H.
Barettino D.
Debray H.
Calvete J.J.
Sanz L.
Institución
Resumen
Parkia platycephala lectin 2 was purified from Parkia platycephala (Leguminosae, Mimosoideae) seeds by affinity chromatography and RP-HPLC. Equilibrium sedimentation and MS showed that Parkia platycephala lectin 2 is a nonglycosylated monomeric protein of molecular mass 29 407 ± 15 Da, which contains six cysteine residues engaged in the formation of three intramolecular disulfide bonds. Parkia platycephala lectin 2 agglutinated rabbit erythrocytes, and this activity was specifically inhibited by N-acetylglucosamine. In addition, Parkia platycephala lectin 2 hydrolyzed β(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-β-d-glucopyranose units in chitin. The full-length amino acid sequence of Parkia platycephala lectin 2, determined by N-terminal sequencing and cDNA cloning, and its three-dimensional structure, established by X-ray crystallography at 1.75 Å resolution, showed that Parkia platycephala lectin 2 is homologous to endochitinases of the glycosyl hydrolase family 18, which share the (βα)8 barrel topology harboring the catalytic residues Asp125, Glu127, and Tyr182. © 2006 The Authors. 273 17 3962 3974 Van Damme, E.J.M., Peumans, W.J., Barre, A., Rougé, P., Plant lectins: A composite of several distinct families of structurally and evolutionary related proteins with diverse biological roles (1998) Crit Rev Plant Sci, 17, pp. 575-692 Gabius, H.-J., Gabius, S., (1997) Glycoscience. 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