This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2jh1

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 22:01, 9 September 2015

CRYSTAL STRUCTURE OF TOXOPLASMA GONDII MICRONEMAL PROTEIN 1

Structural highlights

2jh1 is a 1 chain structure with sequence from Toxgo. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	2bvb, 2jh7, 2jhd
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2jh1"

@@ Line 2: / Line 2: @@
 <StructureSection load='2jh1' size='340' side='right' caption='[[2jh1]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2jh1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JH1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JH1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2jh1]] 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=2JH1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JH1 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></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bvb|2bvb]], [[2jh7|2jh7]], [[2jhd|2jhd]]</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=2jh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jh1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jh1 RCSB], [http://www.ebi.ac.uk/pdbsum/2jh1 PDBsum]</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=2jh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jh1 OCA], [http://pdbe.org/2jh1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jh1 RCSB], [http://www.ebi.ac.uk/pdbsum/2jh1 PDBsum]</span></td></tr>
 </table>
+== 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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 25: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2jh1" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Toxoplasma gondii]]
+[[Category: Toxgo]]
 [[Category: Blackman, M J]]
 [[Category: Blumenschein, T M.A]]

2jh1

From Proteopedia

Revision as of 22:01, 9 September 2015

CRYSTAL STRUCTURE OF TOXOPLASMA GONDII MICRONEMAL PROTEIN 1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox