2gsj
From Proteopedia
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|PDB= 2gsj |SIZE=350|CAPTION= <scene name='initialview01'>2gsj</scene>, resolution 1.73Å | |PDB= 2gsj |SIZE=350|CAPTION= <scene name='initialview01'>2gsj</scene>, resolution 1.73Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gsj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gsj OCA], [http://www.ebi.ac.uk/pdbsum/2gsj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2gsj RCSB]</span> | ||
}} | }} | ||
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[[Category: Souza, E P.de.]] | [[Category: Souza, E P.de.]] | ||
[[Category: Toyama, M H.]] | [[Category: Toyama, M H.]] | ||
| - | [[Category: SO4]] | ||
[[Category: chimerolectin]] | [[Category: chimerolectin]] | ||
[[Category: endochitinase]] | [[Category: endochitinase]] | ||
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[[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 Mon Mar 31 03:20:59 2008'' |
Revision as of 00:20, 31 March 2008
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| , resolution 1.73Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mon Mar 31 03:20:59 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. | Chimerolectin | Endochitinase | Equilibrium sedimentation | Glycosyl hydrolase family 18 | Mimosoideae | X-ray crystal structure
