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| - | ==CRYSTAL STRUCTURE OF TOXOPLASMA GONDII MICRONEMAL PROTEIN 1 BOUND TO 3'-SIALYL-N-ACETYLLACTOSAMINE== | + | |
| - | <StructureSection load='2jhd' size='340' side='right' caption='[[2jhd]], [[Resolution|resolution]] 2.30Å' scene=''> | + | ==Crystal structure of Toxoplasma gondii micronemal protein 1 bound to 3'-sialyl-N-acetyllactosamine== |
| | + | <StructureSection load='2jhd' size='340' side='right'caption='[[2jhd]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2jhd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Toxgo Toxgo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JHD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JHD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2jhd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JHD FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bvb|2bvb]], [[2jh1|2jh1]], [[2jh7|2jh7]]</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=2jhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jhd OCA], [https://pdbe.org/2jhd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jhd RCSB], [https://www.ebi.ac.uk/pdbsum/2jhd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jhd ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jhd OCA], [http://pdbe.org/2jhd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jhd RCSB], [http://www.ebi.ac.uk/pdbsum/2jhd PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MIC1_TOXGO MIC1_TOXGO]] Adhesin. Required for attachment of the parasite to the host cell prior to invasion. Ensures correct folding of MIC6 and transport of the MIC6-MIC1-MIC4 complex into the micronemes.<ref>PMID:11447133</ref> <ref>PMID:11157983</ref> <ref>PMID:16166092</ref> <ref>PMID:17491595</ref> <ref>PMID:9027753</ref> | + | [https://www.uniprot.org/uniprot/MIC1_TOXGO MIC1_TOXGO] Adhesin. Required for attachment of the parasite to the host cell prior to invasion. Ensures correct folding of MIC6 and transport of the MIC6-MIC1-MIC4 complex into the micronemes.<ref>PMID:11447133</ref> <ref>PMID:11157983</ref> <ref>PMID:16166092</ref> <ref>PMID:17491595</ref> <ref>PMID:9027753</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jh/2jhd_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jh/2jhd_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </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/chain_selection.php?pdb_ID=2ata ConSurf]. | + | </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=2jhd ConSurf]. |
| | <div style="clear:both"></div> | | <div style="clear:both"></div> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Toxgo]] | + | [[Category: Large Structures]] |
| - | [[Category: Blackman, M J]] | + | [[Category: Toxoplasma gondii]] |
| - | [[Category: Blumenschein, T M.A]] | + | [[Category: Blackman MJ]] |
| - | [[Category: Campanero-Rhodes, M A]] | + | [[Category: Blumenschein TMA]] |
| - | [[Category: Carpenter, E P]] | + | [[Category: Campanero-Rhodes MA]] |
| - | [[Category: Childs, R A]] | + | [[Category: Carpenter EP]] |
| - | [[Category: Feizi, T]] | + | [[Category: Childs RA]] |
| - | [[Category: Friedrich, N]] | + | [[Category: Feizi T]] |
| - | [[Category: Koutroukides, T]] | + | [[Category: Friedrich N]] |
| - | [[Category: Matthews, S]] | + | [[Category: Koutroukides T]] |
| - | [[Category: Saouros, S]] | + | [[Category: Matthews S]] |
| - | [[Category: Simpson, P]] | + | [[Category: Saouros S]] |
| - | [[Category: Soldati-Favre, D]] | + | [[Category: Simpson P]] |
| - | [[Category: Cell adhesion]]
| + | [[Category: Soldati-Favre D]] |
| - | [[Category: Cell invasion]]
| + | |
| - | [[Category: Mar domain]]
| + | |
| - | [[Category: Mic1]]
| + | |
| - | [[Category: Microneme]]
| + | |
| Structural highlights
2jhd is a 1 chain structure with sequence from Toxoplasma gondii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.3Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
MIC1_TOXGO Adhesin. Required for attachment of the parasite to the host cell prior to invasion. Ensures correct folding of MIC6 and transport of the MIC6-MIC1-MIC4 complex into the micronemes.[1] [2] [3] [4] [5]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The obligate intracellular parasite Toxoplasma gondii, a member of the phylum Apicomplexa that includes Plasmodium spp., is one of the most widespread parasites and the causative agent of toxoplasmosis. Micronemal proteins (MICs) are released onto the parasite surface just before invasion of host cells and play important roles in host cell recognition, attachment and penetration. Here, we report the atomic structure for a key MIC, TgMIC1, and reveal a novel cell-binding motif called the microneme adhesive repeat (MAR). Using glycoarray analyses, we identified a novel interaction with sialylated oligosaccharides that resolves several prevailing misconceptions concerning TgMIC1. Structural studies of various complexes between TgMIC1 and sialylated oligosaccharides provide high-resolution insights into the recognition of sialylated oligosaccharides by a parasite surface protein. We observe that MAR domains exist in tandem repeats, which provide a highly specialized structure for glycan discrimination. Our work uncovers new features of parasite-receptor interactions at the early stages of host cell invasion, which will assist the design of new therapeutic strategies.
Atomic resolution insight into host cell recognition by Toxoplasma gondii.,Blumenschein TM, Friedrich N, Childs RA, Saouros S, Carpenter EP, Campanero-Rhodes MA, Simpson P, Chai W, Koutroukides T, Blackman MJ, Feizi T, Soldati-Favre D, Matthews S EMBO J. 2007 Jun 6;26(11):2808-20. Epub 2007 May 10. PMID:17491595[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lourenco EV, Pereira SR, Faca VM, Coelho-Castelo AA, Mineo JR, Roque-Barreira MC, Greene LJ, Panunto-Castelo A. Toxoplasma gondii micronemal protein MIC1 is a lactose-binding lectin. Glycobiology. 2001 Jul;11(7):541-7. PMID:11447133
- ↑ Reiss M, Viebig N, Brecht S, Fourmaux MN, Soete M, Di Cristina M, Dubremetz JF, Soldati D. Identification and characterization of an escorter for two secretory adhesins in Toxoplasma gondii. J Cell Biol. 2001 Feb 5;152(3):563-78. PMID:11157983
- ↑ Saouros S, Edwards-Jones B, Reiss M, Sawmynaden K, Cota E, Simpson P, Dowse TJ, Jakle U, Ramboarina S, Shivarattan T, Matthews S, Soldati-Favre D. A novel galectin-like domain from Toxoplasma gondii micronemal protein 1 assists the folding, assembly, and transport of a cell adhesion complex. J Biol Chem. 2005 Nov 18;280(46):38583-91. Epub 2005 Sep 15. PMID:16166092 doi:C500365200
- ↑ Blumenschein TM, Friedrich N, Childs RA, Saouros S, Carpenter EP, Campanero-Rhodes MA, Simpson P, Chai W, Koutroukides T, Blackman MJ, Feizi T, Soldati-Favre D, Matthews S. Atomic resolution insight into host cell recognition by Toxoplasma gondii. EMBO J. 2007 Jun 6;26(11):2808-20. Epub 2007 May 10. PMID:17491595
- ↑ Fourmaux MN, Achbarou A, Mercereau-Puijalon O, Biderre C, Briche I, Loyens A, Odberg-Ferragut C, Camus D, Dubremetz JF. The MIC1 microneme protein of Toxoplasma gondii contains a duplicated receptor-like domain and binds to host cell surface. Mol Biochem Parasitol. 1996 Dec 20;83(2):201-10. PMID:9027753
- ↑ Blumenschein TM, Friedrich N, Childs RA, Saouros S, Carpenter EP, Campanero-Rhodes MA, Simpson P, Chai W, Koutroukides T, Blackman MJ, Feizi T, Soldati-Favre D, Matthews S. Atomic resolution insight into host cell recognition by Toxoplasma gondii. EMBO J. 2007 Jun 6;26(11):2808-20. Epub 2007 May 10. PMID:17491595
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