2gsj

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[[Image:2gsj.jpg|left|200px]]
 
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{{Structure
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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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|PDB= 2gsj |SIZE=350|CAPTION= <scene name='initialview01'>2gsj</scene>, resolution 1.73&Aring;
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<StructureSection load='2gsj' size='340' side='right'caption='[[2gsj]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<table><tr><td colspan='2'>[[2gsj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Parkia_platycephala Parkia platycephala]. 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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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.73&#8491;</td></tr>
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|GENE=
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<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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|DOMAIN=
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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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|RELATEDENTRY=
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</table>
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|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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== Evolutionary Conservation ==
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}}
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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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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<jmolCheckbox>
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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/initialview03.spt</scriptWhenUnchecked>
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==Overview==
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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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2GSJ is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Parkia_platycephala Parkia platycephala]. 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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<div class="pdbe-citations 2gsj" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Parkia platycephala]]
[[Category: Parkia platycephala]]
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[[Category: Protein complex]]
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[[Category: Barettino D]]
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[[Category: Barettino, D.]]
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[[Category: Calvete JJ]]
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[[Category: Calvete, J J.]]
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[[Category: Castellon RER]]
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[[Category: Castellon, R E.R.]]
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[[Category: Cavada BS]]
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[[Category: Cavada, B S.]]
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[[Category: Debray H]]
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[[Category: Debray, H.]]
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[[Category: Delatorre P]]
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[[Category: Delatorre, P.]]
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[[Category: Goersch GV]]
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[[Category: Goersch, G V.]]
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[[Category: Leroy Y]]
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[[Category: Jr., W F.de Azevedo.]]
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[[Category: Moreno FB]]
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[[Category: Leroy, Y.]]
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[[Category: Nagano CS]]
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[[Category: Moreno, F B.]]
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[[Category: Nascimento KS]]
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[[Category: Nagano, C S.]]
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[[Category: Pinto VP]]
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[[Category: Nascimento, K S.]]
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[[Category: Radis-Baptista G]]
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[[Category: Pinto, V P.]]
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[[Category: Sampaio AH]]
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[[Category: Radis-Baptista, G.]]
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[[Category: Sanz L]]
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[[Category: Rocha, B A.da.]]
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[[Category: Toyama MH]]
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[[Category: Sampaio, A H.]]
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[[Category: Da Rocha BA]]
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[[Category: Sanz, L.]]
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[[Category: De Azevedo Jr WF]]
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[[Category: Souza, E P.de.]]
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[[Category: De Souza EP]]
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[[Category: Toyama, M H.]]
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[[Category: chimerolectin]]
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[[Category: endochitinase]]
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[[Category: equilibrium sedimentation]]
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[[Category: glycosyl hydrolase family 18]]
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[[Category: mimosoideae]]
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[[Category: parkia platycephala]]
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[[Category: x-ray crystal structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:20:59 2008''
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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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