Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/102796
Type: Artigo de periódico
Title: Cdna Cloning And 1.75 Å Crystal Structure Determination Of Ppl2, An Endochitinase And N-acetylglucosamine-binding Hemagglutinin From Parkia Platycephala Seeds
Author: 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.
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 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.
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Rights: fechado
Identifier DOI: 10.1111/j.1742-4658.2006.05400.x
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-33747413686&partnerID=40&md5=0728f09701b9ea033544acf021a03937
Date Issue: 2006
Appears in Collections:Unicamp - Artigos e Outros Documentos

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