2bvb

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(Difference between revisions)

Revision as of 07:34, 25 June 2021

The C-terminal domain from Micronemal Protein 1 (MIC1) from Toxoplasma Gondii

Structural highlights

2bvb is a 1 chain structure with sequence from Toxgo. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
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]

Publication Abstract from PubMed

Immediately prior to invasion Toxoplasma gondii tachyzoites release a large number of micronemal proteins (TgMICs) that participate in host cell attachment and penetration. The TgMIC4-MIC1-MIC6 complex was the first to be identified in T. gondii and has been recently shown to be critical in invasion. This study establishes that the N-terminal thrombospondin type I repeat-like domains (TSR1-like) from TgMIC1 function as an independent adhesin as well as promoting association with TgMIC4. Using the newly solved three-dimensional structure of the C-terminal domain of TgMIC1 we have identified a novel Galectin-like fold that does not possess carbohydrate binding properties and redefines the architecture of TgMIC1. Instead, the TgMIC1 Galectin-like domain interacts and stabilizes TgMIC6, which provides the basis for a highly specific quality control mechanism for successful exit from the early secretory compartments and for subsequent trafficking of the complex to the micronemes.

A novel galectin-like domain from Toxoplasma gondii micronemal protein 1 assists the folding, assembly, and transport of a cell adhesion complex.,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 J Biol Chem. 2005 Nov 18;280(46):38583-91. Epub 2005 Sep 15. PMID:16166092^[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
↑ 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

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 <StructureSection load='2bvb' size='340' side='right'caption='[[2bvb]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2bvb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Toxgo Toxgo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BVB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BVB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2bvb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Toxgo Toxgo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BVB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BVB FirstGlance]. <br>
-</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=2bvb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bvb OCA], [http://pdbe.org/2bvb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bvb RCSB], [http://www.ebi.ac.uk/pdbsum/2bvb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bvb ProSAT]</span></td></tr>
+</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=2bvb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bvb OCA], [https://pdbe.org/2bvb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bvb RCSB], [https://www.ebi.ac.uk/pdbsum/2bvb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bvb ProSAT]</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>
+[[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

2bvb

From Proteopedia

Revision as of 07:34, 25 June 2021

The C-terminal domain from Micronemal Protein 1 (MIC1) from Toxoplasma Gondii

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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