This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2gsj
From Proteopedia
(New page: 200px<br /><applet load="2gsj" size="350" color="white" frame="true" align="right" spinBox="true" caption="2gsj, resolution 1.73Å" /> '''cDNA cloning and 1.7...) |
|||
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | Parkia platycephala lectin 2 was purified from Parkia platycephala | + | 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== | ||
| Line 14: | Line 14: | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Barettino, D.]] | [[Category: Barettino, D.]] | ||
| - | [[Category: Calvete, J | + | [[Category: Calvete, J J.]] |
| - | [[Category: Castellon, R | + | [[Category: Castellon, R E.R.]] |
| - | [[Category: Cavada, B | + | [[Category: Cavada, B S.]] |
[[Category: Debray, H.]] | [[Category: Debray, H.]] | ||
[[Category: Delatorre, P.]] | [[Category: Delatorre, P.]] | ||
| - | [[Category: Goersch, G | + | [[Category: Goersch, G V.]] |
| - | [[Category: Jr., W | + | [[Category: Jr., W F.de Azevedo.]] |
[[Category: Leroy, Y.]] | [[Category: Leroy, Y.]] | ||
| - | [[Category: Moreno, F | + | [[Category: Moreno, F B.]] |
| - | [[Category: Nagano, C | + | [[Category: Nagano, C S.]] |
| - | [[Category: Nascimento, K | + | [[Category: Nascimento, K S.]] |
| - | [[Category: Pinto, V | + | [[Category: Pinto, V P.]] |
[[Category: Radis-Baptista, G.]] | [[Category: Radis-Baptista, G.]] | ||
| - | [[Category: Rocha, B | + | [[Category: Rocha, B A.da.]] |
| - | [[Category: Sampaio, A | + | [[Category: Sampaio, A H.]] |
[[Category: Sanz, L.]] | [[Category: Sanz, L.]] | ||
| - | [[Category: Souza, E | + | [[Category: Souza, E P.de.]] |
| - | [[Category: Toyama, M | + | [[Category: Toyama, M H.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: chimerolectin]] | [[Category: chimerolectin]] | ||
| Line 41: | Line 41: | ||
[[Category: x-ray crystal structure]] | [[Category: x-ray crystal structure]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''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
|
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
Page seeded by OCA on Thu Feb 21 17:34:53 2008
Categories: Parkia platycephala | Protein complex | Barettino, D. | Calvete, J J. | Castellon, R E.R. | Cavada, B S. | Debray, H. | Delatorre, P. | Goersch, G V. | Jr., W F.de Azevedo. | Leroy, Y. | Moreno, F B. | Nagano, C S. | Nascimento, K S. | Pinto, V P. | Radis-Baptista, G. | Rocha, B A.da. | Sampaio, A H. | Sanz, L. | Souza, E P.de. | Toyama, M H. | SO4 | Chimerolectin | Endochitinase | Equilibrium sedimentation | Glycosyl hydrolase family 18 | Mimosoideae | X-ray crystal structure
