6tu4: Difference between revisions

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<StructureSection load='6tu4' size='340' side='right'caption='[[6tu4]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='6tu4' size='340' side='right'caption='[[6tu4]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6tu4]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Plaf7 Plaf7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TU4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TU4 FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TU4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TU4 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9UE:Jasplakinolide'>9UE</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PFL2215w ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36329 PLAF7])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9UE:Jasplakinolide'>9UE</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=6tu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tu4 OCA], [https://pdbe.org/6tu4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tu4 RCSB], [https://www.ebi.ac.uk/pdbsum/6tu4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tu4 ProSAT]</span></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=6tu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tu4 OCA], [https://pdbe.org/6tu4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tu4 RCSB], [https://www.ebi.ac.uk/pdbsum/6tu4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tu4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/ACT1_PLAF7 ACT1_PLAF7]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Actin assembles into short polymer microfilaments, these are thought to contribute to parasite gliding motility.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Malaria is responsible for half a million deaths annually and poses a huge economic burden on the developing world. The mosquito-borne parasites (Plasmodium spp.) that cause the disease depend upon an unconventional actomyosin motor for both gliding motility and host cell invasion. The motor system, often referred to as the glideosome complex, remains to be understood in molecular terms and is an attractive target for new drugs that might block the infection pathway. Here, we present the high-resolution structure of the actomyosin motor complex from Plasmodium falciparum. The complex includes the malaria parasite actin filament (PfAct1) complexed with the class XIV myosin motor (PfMyoA) and its two associated light-chains. The high-resolution core structure reveals the PfAct1:PfMyoA interface in atomic detail, while at lower-resolution, we visualize the PfMyoA light-chain binding region, including the essential light chain (PfELC) and the myosin tail interacting protein (PfMTIP). Finally, we report a bare PfAct1 filament structure at improved resolution.
High-resolution structures of malaria parasite actomyosin and actin filaments.,Vahokoski J, Calder LJ, Lopez AJ, Molloy JE, Kursula I, Rosenthal PB PLoS Pathog. 2022 Apr 4;18(4):e1010408. doi: 10.1371/journal.ppat.1010408., eCollection 2022 Apr. PMID:35377914<ref>PMID:35377914</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6tu4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Plaf7]]
[[Category: Calder LJ]]
[[Category: Calder, L J]]
[[Category: Kursula I]]
[[Category: Kursula, I]]
[[Category: Lopez AJ]]
[[Category: Lopez, A J]]
[[Category: Rosenthal PB]]
[[Category: Rosenthal, P B]]
[[Category: Vahokoski J]]
[[Category: Vahokoski, J]]
[[Category: Filament]]
[[Category: Malaria]]
[[Category: Motor protein]]
[[Category: Myosin]]
[[Category: Plasmodium falciparum]]
[[Category: Unconventional]]

Latest revision as of 11:52, 14 July 2024

Structure of Plasmodium Actin1 filamentStructure of Plasmodium Actin1 filament

Structural highlights

Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 2.6Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

6tu4, resolution 2.60Å

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OCA
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