2gsj

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(New page: 200px<br /><applet load="2gsj" size="350" color="white" frame="true" align="right" spinBox="true" caption="2gsj, resolution 1.73&Aring;" /> '''cDNA cloning and 1.7...)
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==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Barettino, D.]]
[[Category: Barettino, D.]]
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[[Category: Calvete, J.J.]]
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[[Category: Calvete, J J.]]
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[[Category: Castellon, R.E.R.]]
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[[Category: Castellon, R E.R.]]
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[[Category: Cavada, B.S.]]
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[[Category: Cavada, B S.]]
[[Category: Debray, H.]]
[[Category: Debray, H.]]
[[Category: Delatorre, P.]]
[[Category: Delatorre, P.]]
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[[Category: Goersch, G.V.]]
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[[Category: Goersch, G V.]]
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[[Category: Jr., W.F.de.Azevedo.]]
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[[Category: Jr., W F.de Azevedo.]]
[[Category: Leroy, Y.]]
[[Category: Leroy, Y.]]
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[[Category: Moreno, F.B.]]
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[[Category: Moreno, F B.]]
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[[Category: Nagano, C.S.]]
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[[Category: Nagano, C S.]]
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[[Category: Nascimento, K.S.]]
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[[Category: Nascimento, K S.]]
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[[Category: Pinto, V.P.]]
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[[Category: Pinto, V P.]]
[[Category: Radis-Baptista, G.]]
[[Category: Radis-Baptista, G.]]
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[[Category: Rocha, B.A.da.]]
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[[Category: Rocha, B A.da.]]
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[[Category: Sampaio, A.H.]]
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[[Category: Sampaio, A H.]]
[[Category: Sanz, L.]]
[[Category: Sanz, L.]]
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[[Category: Souza, E.P.de.]]
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[[Category: Souza, E P.de.]]
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[[Category: Toyama, M.H.]]
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[[Category: Toyama, M H.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: chimerolectin]]
[[Category: chimerolectin]]
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[[Category: x-ray crystal structure]]
[[Category: x-ray crystal structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:07:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:34:53 2008''

Revision as of 15:34, 21 February 2008


2gsj, resolution 1.73Å

Drag the structure with the mouse to rotate

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

Overview

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.

About this Structure

2GSJ is a Protein complex structure of sequences from Parkia platycephala with as ligand. Full crystallographic information is available from OCA.

Reference

cDNA cloning and 1.75 A crystal structure determination of PPL2, an endochitinase and N-acetylglucosamine-binding hemagglutinin from Parkia platycephala seeds., Cavada BS, Moreno FB, da Rocha BA, de Azevedo WF Jr, Castellon RE, Goersch GV, Nagano CS, de Souza EP, Nascimento KS, Radis-Baptista G, Delatorre P, Leroy Y, Toyama MH, Pinto VP, Sampaio AH, Barettino D, Debray H, Calvete JJ, Sanz L, FEBS J. 2006 Sep;273(17):3962-74. PMID:16934035

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