2gsj
From Proteopedia
(Difference between revisions)
(8 intermediate revisions not shown.) | |||
Line 1: | Line 1: | ||
- | [[Image:2gsj.png|left|200px]] | ||
- | + | ==cDNA cloning and 1.75A crystal structure determination of PPL2, a novel chimerolectin from Parkia platycephala seeds exhibiting endochitinolytic activity== | |
+ | <StructureSection load='2gsj' size='340' side='right'caption='[[2gsj]], [[Resolution|resolution]] 1.73Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <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> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.73Å</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> | ||
+ | <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> | ||
+ | </table> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gs/2gsj_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </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]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == 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. | ||
- | + | 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> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 2gsj" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | < | + | </StructureSection> |
- | + | [[Category: Large Structures]] | |
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | [[Category: | + | |
[[Category: Parkia platycephala]] | [[Category: Parkia platycephala]] | ||
- | [[Category: | + | [[Category: Barettino D]] |
+ | [[Category: Calvete JJ]] | ||
+ | [[Category: Castellon RER]] | ||
+ | [[Category: Cavada BS]] | ||
+ | [[Category: Debray H]] | ||
+ | [[Category: Delatorre P]] | ||
+ | [[Category: Goersch GV]] | ||
+ | [[Category: Leroy Y]] | ||
+ | [[Category: Moreno FB]] | ||
+ | [[Category: Nagano CS]] | ||
+ | [[Category: Nascimento KS]] | ||
+ | [[Category: Pinto VP]] | ||
+ | [[Category: Radis-Baptista G]] | ||
+ | [[Category: Sampaio AH]] | ||
+ | [[Category: Sanz L]] | ||
+ | [[Category: Toyama MH]] | ||
+ | [[Category: Da Rocha BA]] | ||
+ | [[Category: De Azevedo Jr WF]] | ||
+ | [[Category: De Souza EP]] |
Current revision
cDNA cloning and 1.75A crystal structure determination of PPL2, a novel chimerolectin from Parkia platycephala seeds exhibiting endochitinolytic activity
|
Categories: Large Structures | Parkia platycephala | Barettino D | Calvete JJ | Castellon RER | Cavada BS | Debray H | Delatorre P | Goersch GV | Leroy Y | Moreno FB | Nagano CS | Nascimento KS | Pinto VP | Radis-Baptista G | Sampaio AH | Sanz L | Toyama MH | Da Rocha BA | De Azevedo Jr WF | De Souza EP