2GSJ

cDNA cloning and 1.75A crystal structure determination of PPL2, a novel chimerolectin from Parkia platycephala seeds exhibiting endochitinolytic activity

Summary for 2GSJ

• Entry DOI: 10.2210/pdb2gsj/pdb
• Descriptor: protein PPL-2, SULFATE ION (3 entities in total)
• Functional Keywords: parkia platycephala, mimosoideae, chimerolectin, endochitinase, glycosyl hydrolase family 18, equilibrium sedimentation, x-ray crystal structure, hydrolase
• Biological source: Parkia platycephala
• Total number of polymer chains: 1
• Total formula weight: 29903.27

Authors

Cavada, B.S.,Moreno, F.B.,da Rocha, B.A.,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.,Sampaio, A.H.,Barettino, D.,Debray, H.,Calvete, J.J.,Sanz, L. (deposition date: 2006-04-26, release date: 2007-03-13, Last modification date: 2024-10-09)

Primary citation

Cavada, B.S.,Moreno, F.B.,da Rocha, B.A.,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.,Sampaio, A.H.,Barettino, D.,Debray, H.,Calvete, J.J.,Sanz, L.
cDNA cloning and 1.75 A crystal structure determination of PPL2, an endochitinase and N-acetylglucosamine-binding hemagglutinin from Parkia platycephala seeds
Febs J., 273:3962-3974, 2006

PubMed 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-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 A resolution, showed that Parkia platycephala lectin 2 is homologous to endochitinases of the glycosyl hydrolase family 18, which share the (betaalpha)8 barrel topology harboring the catalytic residues Asp125, Glu127, and Tyr182.

PubMed: 16934035
DOI: 10.1111/j.1742-4658.2006.05400.x

Experimental method

X-RAY DIFFRACTION (1.73 Å)