8c4a: Difference between revisions
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The | ==Structural and interactional insights into the glideosome-associated connector from Toxoplasma gondii== | ||
<StructureSection load='8c4a' size='340' side='right'caption='[[8c4a]], [[Resolution|resolution]] 2.67Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8c4a]] 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=8C4A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8C4A FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.675Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=8c4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8c4a OCA], [https://pdbe.org/8c4a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8c4a RCSB], [https://www.ebi.ac.uk/pdbsum/8c4a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8c4a ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A7J6JYP1_TOXGO A0A7J6JYP1_TOXGO] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The phylum of Apicomplexa groups intracellular parasites that employ substrate-dependent gliding motility to invade host cells, egress from the infected cells, and cross biological barriers. The glideosome-associated connector (GAC) is a conserved protein essential to this process. GAC facilitates the association of actin filaments with surface transmembrane adhesins and the efficient transmission of the force generated by myosin translocation of actin to the cell surface substrate. Here, we present the crystal structure of Toxoplasma gondii GAC and reveal a unique, supercoiled armadillo repeat region that adopts a closed ring conformation. Characterisation of the solution properties together with membrane and F-actin binding interfaces suggests that GAC adopts several conformations from closed to open and extended. A multi-conformational model for assembly and regulation of GAC within the glideosome is proposed. | |||
Structural and regulatory insights into the glideosome-associated connector from Toxoplasma gondii.,Kumar A, Vadas O, Dos Santos Pacheco N, Zhang X, Chao K, Darvill N, Rasmussen HO, Xu Y, Lin GM, Stylianou FA, Pedersen JS, Rouse SL, Morgan ML, Soldati-Favre D, Matthews S Elife. 2023 Apr 4;12:e86049. doi: 10.7554/eLife.86049. PMID:37014051<ref>PMID:37014051</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8c4a" style="background-color:#fffaf0;"></div> | ||
[[Category: Kumar | == References == | ||
[[Category: Morgan | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Toxoplasma gondii]] | |||
[[Category: Kumar A]] | |||
[[Category: Matthews SJ]] | |||
[[Category: Morgan RML]] | |||
Latest revision as of 09:11, 19 July 2023
Structural and interactional insights into the glideosome-associated connector from Toxoplasma gondiiStructural and interactional insights into the glideosome-associated connector from Toxoplasma gondii
Structural highlights
FunctionPublication Abstract from PubMedThe phylum of Apicomplexa groups intracellular parasites that employ substrate-dependent gliding motility to invade host cells, egress from the infected cells, and cross biological barriers. The glideosome-associated connector (GAC) is a conserved protein essential to this process. GAC facilitates the association of actin filaments with surface transmembrane adhesins and the efficient transmission of the force generated by myosin translocation of actin to the cell surface substrate. Here, we present the crystal structure of Toxoplasma gondii GAC and reveal a unique, supercoiled armadillo repeat region that adopts a closed ring conformation. Characterisation of the solution properties together with membrane and F-actin binding interfaces suggests that GAC adopts several conformations from closed to open and extended. A multi-conformational model for assembly and regulation of GAC within the glideosome is proposed. Structural and regulatory insights into the glideosome-associated connector from Toxoplasma gondii.,Kumar A, Vadas O, Dos Santos Pacheco N, Zhang X, Chao K, Darvill N, Rasmussen HO, Xu Y, Lin GM, Stylianou FA, Pedersen JS, Rouse SL, Morgan ML, Soldati-Favre D, Matthews S Elife. 2023 Apr 4;12:e86049. doi: 10.7554/eLife.86049. PMID:37014051[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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