6v6a: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='6v6a' size='340' side='right'caption='[[6v6a]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='6v6a' size='340' side='right'caption='[[6v6a]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6v6a]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6v6a]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Toxoplasma_gondii_RH Toxoplasma gondii RH]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V6A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6V6A FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=6v6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v6a OCA], [https://pdbe.org/6v6a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6v6a RCSB], [https://www.ebi.ac.uk/pdbsum/6v6a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6v6a ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q2QDG8_TOXGO Q2QDG8_TOXGO] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 18: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 6v6a" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6v6a" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Mitogen-activated protein kinase 3D structures|Mitogen-activated protein kinase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 23: | Line 27: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Toxoplasma gondii RH]] | |||
[[Category: Toxoplasma gondii | [[Category: Back PS]] | ||
[[Category: Back | [[Category: Bradley PJ]] | ||
[[Category: Bradley | [[Category: Dewangan PS]] | ||
[[Category: Dewangan | [[Category: Hu X]] | ||
[[Category: Hu | [[Category: O'Shaughnessy WJ]] | ||
[[Category: | [[Category: Reese ML]] | ||
[[Category: | |||
Latest revision as of 11:04, 11 October 2023
Inhibitory scaffolding of the ancient MAPK, ERK7Inhibitory scaffolding of the ancient MAPK, ERK7
Structural highlights
FunctionPublication Abstract from PubMedApicomplexan parasites use a specialized cilium structure called the apical complex to organize their secretory organelles and invasion machinery. The apical complex is integrally associated with both the parasite plasma membrane and an intermediate filament cytoskeleton called the inner-membrane complex (IMC). While the apical complex is essential to the parasitic lifestyle, little is known about the regulation of apical complex biogenesis. Here, we identify AC9 (apical cap protein 9), a largely intrinsically disordered component of the Toxoplasma gondii IMC, as essential for apical complex development, and therefore for host cell invasion and egress. Parasites lacking AC9 fail to successfully assemble the tubulin-rich core of their apical complex, called the conoid. We use proximity biotinylation to identify the AC9 interaction network, which includes the kinase extracellular signal-regulated kinase 7 (ERK7). Like AC9, ERK7 is required for apical complex biogenesis. We demonstrate that AC9 directly binds ERK7 through a conserved C-terminal motif and that this interaction is essential for ERK7 localization and function at the apical cap. The crystal structure of the ERK7-AC9 complex reveals that AC9 is not only a scaffold but also inhibits ERK7 through an unusual set of contacts that displaces nucleotide from the kinase active site. ERK7 is an ancient and autoactivating member of the mitogen-activated kinase (MAPK) family and its regulation is poorly understood in all organisms. We propose that AC9 dually regulates ERK7 by scaffolding and concentrating it at its site of action while maintaining it in an "off" state until the specific binding of a true substrate. Ancient MAPK ERK7 is regulated by an unusual inhibitory scaffold required for Toxoplasma apical complex biogenesis.,Back PS, O'Shaughnessy WJ, Moon AS, Dewangan PS, Hu X, Sha J, Wohlschlegel JA, Bradley PJ, Reese ML Proc Natl Acad Sci U S A. 2020 May 14. pii: 1921245117. doi:, 10.1073/pnas.1921245117. PMID:32409604[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||