1vcl

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[[Image:1vcl.gif|left|200px]]
 
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{{Structure
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==Crystal Structure of Hemolytic Lectin CEL-III==
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|PDB= 1vcl |SIZE=350|CAPTION= <scene name='initialview01'>1vcl</scene>, resolution 1.70&Aring;
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<StructureSection load='1vcl' size='340' side='right'caption='[[1vcl]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>
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<table><tr><td colspan='2'>[[1vcl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cucumaria_echinata Cucumaria echinata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VCL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VCL 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]] 1.7&#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=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</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=1vcl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vcl OCA], [https://pdbe.org/1vcl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vcl RCSB], [https://www.ebi.ac.uk/pdbsum/1vcl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vcl 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=1vcl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vcl OCA], [http://www.ebi.ac.uk/pdbsum/1vcl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vcl RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/CEL3_CUCEC CEL3_CUCEC] Galactose/N-acetylgalactosamine (Gal/GalNAc)-binding lectin with hemolytic activity. Favors saccharides that have a beta-1,4 linkage at the non-reducing end rather than saccharides having alpha-1,6 or alpha-1,4 linkages. Binds lactose, lactulose, GalNAc, galactosamine, methyl alpha-galactopyranoside, methyl beta-galactopyranoside, N-acetyllactosamine, p-nitrophenyl beta-D-galactopyranoside (pNP-Gal), p-nitrophenyl N-acetyl-beta-D-galactosaminide (pNP-GalNAc), asialofetuin, and human erythrocyte membrane lipids lactosyl ceramide (LacCer) and globoside globotetraosylceramide (Gb4Cer). Binds moderately to galactose, melibiose, raffinose, fucose, methyl alpha-galactoside and methyl beta-galactoside. Binds weakly to glucose, mannose and N-acetylglucosamine (GlcNAc) (PubMed:10101284, PubMed:10478454, PubMed:10923802, PubMed:11471734, PubMed:11983084, PubMed:14561725, PubMed:15194688, PubMed:17977832, PubMed:18159942, PubMed:19356139, PubMed:19420692, PubMed:22313748, PubMed:23470749, PubMed:23545649, PubMed:23583369, PubMed:24652284, PubMed:27101707, PubMed:7798179, PubMed:7876091, PubMed:8663224, PubMed:9058193, PubMed:9133626, PubMed:9305736, PubMed:9692203, PubMed:9805377, PubMed:9990124). Has hemolytic activity towards human (A, B and O-type), rabbit and rat erythrocytes, but not towards mouse, chicken or horse erythrocytes (PubMed:10101284, PubMed:10923802, PubMed:11471734, PubMed:18159942, PubMed:19356139, PubMed:19420692, PubMed:22313748, PubMed:23583369, PubMed:27101707, PubMed:7798179, PubMed:7876091, PubMed:8663224, PubMed:9058193, PubMed:9692203, PubMed:9805377). Forms ion-permeable transmembrane pores in the erythrocyte membrane as well as in artificial liposomes containing human erythrocyte membrane lipids LacCer, Gb4Cer and galactosyl ceramide (GalCer) leading to destruction of the membrane (PubMed:10478454, PubMed:7876091, PubMed:9133626, PubMed:9990124). Has hemagglutinating activity towards rabbit, human and rat erythrocytes, and at relatively high concentrations towards chicken and horse erythrocytes, but not towards mouse erythrocytes (PubMed:10923802, PubMed:11471734, PubMed:14561725, PubMed:18159942, PubMed:19420692, PubMed:7798179, PubMed:9692203, PubMed:9805377, PubMed:9990124). Has dose-dependent cytotoxic effect on Madin-Darby canine kidney (MDCK), African green monkey kidney (Vero) and human epithelia carcinoma (HeLa) cell lines, but Chinese hamster ovary (CHO), rat sarcoma (XC) and potoroo rat kangaroo kidney (PtK1) cells are highly resistant to the cytotoxic effect of this protein (PubMed:10101284, PubMed:9133626). Impairs malaria parasite development in malaria parasite infected transgenic A.stephensi mosquitoes expressing this protein specifically in their midguts. Binds to ookinetes and leads to strong dose-dependent inhibition of ookinete formation in vitro. Leads to severely impaired oocyst formation and significantly reduced sporozoite production of rodent malaria parasite P.berghei in the salivary glands of the transgenic mosquitoes. The parasite transmission to uninfected mice (vectorial competence) of these mosquitoes is significantly impaired. Leads also to severely impaired oocyst formation of human malaria parasite P.falciparum in transgenic mosquitoes fed on mature P.falciparum gametocyte cultures (PubMed:18159942). May be involved in defense mechanisms acting as a toxic protein to foreign microorganisms (PubMed:7876091, PubMed:9133626). May act in defense against predators (PubMed:24652284).<ref>PMID:10101284</ref> <ref>PMID:10478454</ref> <ref>PMID:10923802</ref> <ref>PMID:11471734</ref> <ref>PMID:11983084</ref> <ref>PMID:14561725</ref> <ref>PMID:15194688</ref> <ref>PMID:17977832</ref> <ref>PMID:18159942</ref> <ref>PMID:19356139</ref> <ref>PMID:19420692</ref> <ref>PMID:22313748</ref> <ref>PMID:23470749</ref> <ref>PMID:23545649</ref> <ref>PMID:23583369</ref> <ref>PMID:24652284</ref> <ref>PMID:27101707</ref> <ref>PMID:7798179</ref> <ref>PMID:7876091</ref> <ref>PMID:8663224</ref> <ref>PMID:9058193</ref> <ref>PMID:9133626</ref> <ref>PMID:9305736</ref> <ref>PMID:9692203</ref> <ref>PMID:9805377</ref> <ref>PMID:9990124</ref>
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== Evolutionary Conservation ==
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'''Crystal Structure of Hemolytic Lectin CEL-III'''
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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/vc/1vcl_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1vcl 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 ==
CEL-III is a Ca(2+)-dependent and galactose-specific lectin purified from the sea cucumber, Cucumaria echinata, which exhibits hemolytic and hemagglutinating activities. Six molecules of CEL-III are assumed to oligomerize to form an ion-permeable pore in the cell membrane. We have determined the crystal structure of CELIII by using single isomorphous replacement aided by anomalous scattering in lead at 1.7 A resolution. CEL-III consists of three distinct domains as follows: the N-terminal two carbohydrate-binding domains (1 and 2), which adopt beta-trefoil folds such as the B-chain of ricin and are members of the (QXW)(3) motif family; and domain 3, which is a novel fold composed of two alpha-helices and one beta-sandwich. CEL-III is the first Ca(2+)-dependent lectin structure with two beta-trefoil folds. Despite sharing the structure of the B-chain of ricin, CEL-III binds five Ca(2+) ions at five of the six subdomains in both domains 1 and 2. Considering the relatively high similarity among the five subdomains, they are putative binding sites for galactose-related carbohydrates, although it remains to be elucidated whether bound Ca(2+) is directly involved in interaction with carbohydrates. The paucity of hydrophobic interactions in the interfaces between the domains and biochemical data suggest that these domains rearrange upon carbohydrate binding in the erythrocyte membrane. This conformational change may be responsible for oligomerization of CEL-III molecules and hemolysis in the erythrocyte membranes.
CEL-III is a Ca(2+)-dependent and galactose-specific lectin purified from the sea cucumber, Cucumaria echinata, which exhibits hemolytic and hemagglutinating activities. Six molecules of CEL-III are assumed to oligomerize to form an ion-permeable pore in the cell membrane. We have determined the crystal structure of CELIII by using single isomorphous replacement aided by anomalous scattering in lead at 1.7 A resolution. CEL-III consists of three distinct domains as follows: the N-terminal two carbohydrate-binding domains (1 and 2), which adopt beta-trefoil folds such as the B-chain of ricin and are members of the (QXW)(3) motif family; and domain 3, which is a novel fold composed of two alpha-helices and one beta-sandwich. CEL-III is the first Ca(2+)-dependent lectin structure with two beta-trefoil folds. Despite sharing the structure of the B-chain of ricin, CEL-III binds five Ca(2+) ions at five of the six subdomains in both domains 1 and 2. Considering the relatively high similarity among the five subdomains, they are putative binding sites for galactose-related carbohydrates, although it remains to be elucidated whether bound Ca(2+) is directly involved in interaction with carbohydrates. The paucity of hydrophobic interactions in the interfaces between the domains and biochemical data suggest that these domains rearrange upon carbohydrate binding in the erythrocyte membrane. This conformational change may be responsible for oligomerization of CEL-III molecules and hemolysis in the erythrocyte membranes.
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==About this Structure==
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Crystal structure of the hemolytic lectin CEL-III isolated from the marine invertebrate Cucumaria echinata: implications of domain structure for its membrane pore-formation mechanism.,Uchida T, Yamasaki T, Eto S, Sugawara H, Kurisu G, Nakagawa A, Kusunoki M, Hatakeyama T J Biol Chem. 2004 Aug 27;279(35):37133-41. Epub 2004 Jun 11. PMID:15194688<ref>PMID:15194688</ref>
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1VCL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Cucumaria_echinata Cucumaria echinata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VCL 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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Crystal structure of the hemolytic lectin CEL-III isolated from the marine invertebrate Cucumaria echinata: implications of domain structure for its membrane pore-formation mechanism., Uchida T, Yamasaki T, Eto S, Sugawara H, Kurisu G, Nakagawa A, Kusunoki M, Hatakeyama T, J Biol Chem. 2004 Aug 27;279(35):37133-41. Epub 2004 Jun 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15194688 15194688]
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</div>
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<div class="pdbe-citations 1vcl" 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>
[[Category: Cucumaria echinata]]
[[Category: Cucumaria echinata]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Eto, S.]]
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[[Category: Eto S]]
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[[Category: Hatakeyama, T.]]
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[[Category: Hatakeyama T]]
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[[Category: Kurisu, G.]]
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[[Category: Kurisu G]]
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[[Category: Kusunoki, M.]]
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[[Category: Kusunoki M]]
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[[Category: Nakagawa, A.]]
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[[Category: Nakagawa A]]
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[[Category: Sugawara, H.]]
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[[Category: Sugawara H]]
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[[Category: Uchida, T.]]
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[[Category: Uchida T]]
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[[Category: Yamasaki, T.]]
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[[Category: Yamasaki T]]
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[[Category: calcium]]
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[[Category: cel-iii]]
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[[Category: hemagglutination]]
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[[Category: hemolysis]]
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[[Category: lectin]]
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[[Category: pore-forming]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:22:29 2008''
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Current revision

Crystal Structure of Hemolytic Lectin CEL-III

PDB ID 1vcl

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