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Type: Artigo de periódico
Title: cDNA cloning and 1.75 angstrom crystal structure determination of PPL2, an endochitinase and N-acetylglucosamine-binding hemagglutinin from Parkia platycephala seeds
Author: Cavada, BS
Moreno, FBB
da Rocha, BAM
de Azevedo, WF
Castellon, RER
Goersch, GV
Nagano, CS
de Souza, EP
Nascimento, KS
Radis-Baptista, G
Delatorre, P
Leroy, Y
Toyama, MH
Pinto, VPT
Sampaio, AH
Barettino, D
Debray, H
Calvete, JJ
Sanz, L
Abstract: 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 beta(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-beta-D-glucopyranose units in chitin. The full-lengthamino 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 angstrom resolution, showed that Parkia platycephala lectin 2 is homologous to endochitinases of the glycosyl hydrolase family 18, which share the (beta alpha)(8) barrel topology harboring the catalytic residues Asp125, Glu127, and Tyr182.
Subject: endochitinase
glycosyl hydrolase family 18
Parkia platycephala
X-ray crystal structure
Country: Inglaterra
Editor: Blackwell Publishing
Rights: fechado
Identifier DOI: 10.1111/j.1742-4658.2006.0540.x
Date Issue: 2006
Appears in Collections:Unicamp - Artigos e Outros Documentos

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