cDNA cloning and 1.75 Å crystal structure determination of PPL2, an endochitinase and N-acetylglucosamine-binding hemagglutinin from Parkia platycephala seeds
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Wiley
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Resumo
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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Endochitinase , Glycosyl hydrolase family 18 , Mimosoideae , Parkia platycephala , X-ray crystal structure , chitin , chitinase , complementary DNA , endochitinase , genomic DNA , glycosidase , hemagglutinin , lectin , lectin 2 , n acetylglucosamine , RNA , unclassified drug , affinity chromatography , amino acid composition , amino acid sequence , animal cell , anion exchange chromatography , controlled study , crystal structure , disulfide bond , enzyme activity , enzyme analysis , enzyme inhibition , enzyme purification , erythrocyte , hemagglutination , legume , matrix assisted laser desorption ionization time of flight mass spectrometry , molecular cloning , molecular weight , nonhuman , polyacrylamide gel electrophoresis , priority journal , rabbit , reversed phase high performance liquid chromatography , RNA isolation , sedimentation , X ray crystallography , Acetylglucosamine , Amino Acid Sequence , Base Sequence , Chitinase , Cloning, Molecular , Crystallization , Crystallography, X-Ray , DNA, Complementary , Fabaceae , Hemagglutinins , Molecular Sequence Data , Plant Lectins , Protein Binding , Seeds , Oryctolagus cuniculus
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Inglês
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FEBS Journal, v. 273, n. 17, p. 3962-3974, 2006.
