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1ulm

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[[Image:1ulm.png|left|200px]]
 
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{{STRUCTURE_1ulm| PDB=1ulm | SCENE= }}
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==Crystal Structure of Pokeweed Lectin-D2 complexed with tri-N-acetylchitotriose==
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<StructureSection load='1ulm' size='340' side='right'caption='[[1ulm]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ulm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Phytolacca_americana Phytolacca americana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ULM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ULM FirstGlance]. <br>
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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]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900017:triacetyl-beta-chitotriose'>PRD_900017</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=1ulm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ulm OCA], [https://pdbe.org/1ulm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ulm RCSB], [https://www.ebi.ac.uk/pdbsum/1ulm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ulm ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LED2_PHYAM LED2_PHYAM] N-acetyl-D-glucosamine binding lectin. Shows no hemagglutinating activity towards rabbit erythrocytes and weak activity towards trypsin-treated erythrocytes. Has mitogenic activity towards human peripheral blood lymphocytes (HPBL).<ref>PMID:8987560</ref> <ref>PMID:15277769</ref> <ref>PMID:14623194</ref>
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== Evolutionary Conservation ==
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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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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ul/1ulm_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=1ulm 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 ==
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The roots of pokeweed (Phytolacca americana) are known to contain the lectins designated PL-A, PL-B, PL-C, PL-D1, and PL-D2. Of these lectins, the crystal structures of two PLs, the ligand-free PL-C and the complex of PL-D2 with tri-N-acetylchitotriose, have been determined at 1.8A resolution. The polypeptide chains of PL-C and PL-D2 form three and two repetitive chitin-binding domains, respectively. In the crystal structure of the PL-D2 complex, one trisaccharide molecule is shared mainly between two neighboring molecules related to each other by a crystallographic 2(1)-screw axis, and infinite helical chains of complexed molecules are generated by the sharing of ligand molecules. The crystal structure of PL-C reveals that the molecule is a dimer of two identical subunits, whose polypeptide chains are located in a head-to-tail fashion by a molecular 2-fold axis. Three putative carbohydrate-binding sites in each subunit are located in the dimer interface. The dimerization of PL-C is performed through the hydrophobic interactions between the carbohydrate-binding sites of the opposite domains in the dimer, leading to a distinct dimerization mode from that of wheat-germ agglutinin. Three aromatic residues in each carbohydrate-binding site of PL-C are involved in the dimerization. These residues correspond to the residues that interact mainly with the trisaccharide in the PL-D2 complex and appear to mimic the saccharide residues in the complex. Consequently, the present structure of the PL-C dimer has no room for accommodating carbohydrate. The quaternary structure of PL-C formed through these putative carbohydrate-binding residues may lead to the lack of hemagglutinating activity.
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===Crystal Structure of Pokeweed Lectin-D2 complexed with tri-N-acetylchitotriose===
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Similarity between protein-protein and protein-carbohydrate interactions, revealed by two crystal structures of lectins from the roots of pokeweed.,Hayashida M, Fujii T, Hamasu M, Ishiguro M, Hata Y J Mol Biol. 2003 Nov 28;334(3):551-65. PMID:14623194<ref>PMID:14623194</ref>
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{{ABSTRACT_PUBMED_14623194}}
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==About this Structure==
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<div class="pdbe-citations 1ulm" style="background-color:#fffaf0;"></div>
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[[1ulm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Phytolacca_americana Phytolacca americana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ULM OCA].
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== References ==
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<references/>
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==Reference==
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__TOC__
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<ref group="xtra">PMID:014623194</ref><references group="xtra"/>
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Phytolacca americana]]
[[Category: Phytolacca americana]]
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[[Category: Fujii, T.]]
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[[Category: Fujii T]]
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[[Category: Hata, Y.]]
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[[Category: Hata Y]]
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[[Category: Hayashida, M.]]
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[[Category: Hayashida M]]
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[[Category: Ishiguro, M.]]
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[[Category: Ishiguro M]]
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[[Category: Chitin-binding]]
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[[Category: Hevein domain]]
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[[Category: Lectin]]
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[[Category: Sugar binding protein]]
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Current revision

Crystal Structure of Pokeweed Lectin-D2 complexed with tri-N-acetylchitotriose

PDB ID 1ulm

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