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2gsj

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[[Image:2gsj.jpg|left|200px]]
 
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==cDNA cloning and 1.75A crystal structure determination of PPL2, a novel chimerolectin from Parkia platycephala seeds exhibiting endochitinolytic activity==
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The line below this paragraph, containing "STRUCTURE_2gsj", creates the "Structure Box" on the page.
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<StructureSection load='2gsj' size='340' side='right'caption='[[2gsj]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2gsj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Parpc Parpc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GSJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GSJ FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gsj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gsj OCA], [https://pdbe.org/2gsj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gsj RCSB], [https://www.ebi.ac.uk/pdbsum/2gsj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gsj ProSAT]</span></td></tr>
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{{STRUCTURE_2gsj| PDB=2gsj | SCENE= }}
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</table>
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== Evolutionary Conservation ==
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'''cDNA cloning and 1.75A crystal structure determination of PPL2, a novel chimerolectin from Parkia platycephala seeds exhibiting endochitinolytic activity'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gs/2gsj_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2gsj ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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.
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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==About this Structure==
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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<ref>PMID:16934035</ref>
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GSJ OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16934035 16934035]
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</div>
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[[Category: Barettino, D.]]
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<div class="pdbe-citations 2gsj" style="background-color:#fffaf0;"></div>
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[[Category: Calvete, J J.]]
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== References ==
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[[Category: Castellon, R E.R.]]
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<references/>
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[[Category: Cavada, B S.]]
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__TOC__
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[[Category: Debray, H.]]
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</StructureSection>
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[[Category: Delatorre, P.]]
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[[Category: Large Structures]]
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[[Category: Goersch, G V.]]
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[[Category: Parpc]]
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[[Category: Jr., W F.de Azevedo.]]
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[[Category: Azevedo, W F.de]]
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[[Category: Leroy, Y.]]
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[[Category: Barettino, D]]
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[[Category: Moreno, F B.]]
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[[Category: Calvete, J J]]
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[[Category: Nagano, C S.]]
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[[Category: Castellon, R E.R]]
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[[Category: Nascimento, K S.]]
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[[Category: Cavada, B S]]
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[[Category: Pinto, V P.]]
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[[Category: Debray, H]]
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[[Category: Radis-Baptista, G.]]
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[[Category: Delatorre, P]]
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[[Category: Rocha, B A.da.]]
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[[Category: Goersch, G V]]
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[[Category: Sampaio, A H.]]
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[[Category: Leroy, Y]]
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[[Category: Sanz, L.]]
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[[Category: Moreno, F B]]
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[[Category: Souza, E P.de.]]
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[[Category: Nagano, C S]]
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[[Category: Toyama, M H.]]
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[[Category: Nascimento, K S]]
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[[Category: Pinto, V P]]
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[[Category: Radis-Baptista, G]]
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[[Category: Rocha, B A.da]]
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[[Category: Sampaio, A H]]
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[[Category: Sanz, L]]
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[[Category: Souza, E P.de]]
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[[Category: Toyama, M H]]
[[Category: Chimerolectin]]
[[Category: Chimerolectin]]
[[Category: Endochitinase]]
[[Category: Endochitinase]]
[[Category: Equilibrium sedimentation]]
[[Category: Equilibrium sedimentation]]
[[Category: Glycosyl hydrolase family 18]]
[[Category: Glycosyl hydrolase family 18]]
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[[Category: Hydrolase]]
[[Category: Mimosoideae]]
[[Category: Mimosoideae]]
[[Category: Parkia platycephala]]
[[Category: Parkia platycephala]]
[[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 Sun May 4 05:28:35 2008''
 

Current revision

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

PDB ID 2gsj

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