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| | <SX load='5ogw' size='340' side='right' viewer='molstar' caption='[[5ogw]], [[Resolution|resolution]] 3.80Å' scene=''> | | <SX load='5ogw' size='340' side='right' viewer='molstar' caption='[[5ogw]], [[Resolution|resolution]] 3.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ogw]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Plafx Plafx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OGW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5OGW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ogw]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_HB3 Plasmodium falciparum HB3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OGW 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='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'>[http://proteopedia.org/fgij/fg.htm?mol=5ogw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ogw OCA], [http://pdbe.org/5ogw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ogw RCSB], [http://www.ebi.ac.uk/pdbsum/5ogw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ogw 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=5ogw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ogw OCA], [https://pdbe.org/5ogw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ogw RCSB], [https://www.ebi.ac.uk/pdbsum/5ogw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ogw ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ACT1_PLAFX ACT1_PLAFX]] 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. | + | [https://www.uniprot.org/uniprot/ACT1_PLAFX ACT1_PLAFX] 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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </SX> | | </SX> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Plafx]] | + | [[Category: Plasmodium falciparum HB3]] |
| - | [[Category: Ecken, J von der]]
| + | [[Category: Kumpula E-P]] |
| - | [[Category: Kumpula, E P]] | + | [[Category: Kursula I]] |
| - | [[Category: Kursula, I]] | + | [[Category: Pospich S]] |
| - | [[Category: Pospich, S]] | + | [[Category: Raunser S]] |
| - | [[Category: Raunser, S]] | + | [[Category: Vahokoski J]] |
| - | [[Category: Vahokoski, J]] | + | [[Category: Von der Ecken J]] |
| - | [[Category: Cryo-em]] | + | |
| - | [[Category: Cytoskeleton]]
| + | |
| - | [[Category: F-actin]]
| + | |
| - | [[Category: Filament]]
| + | |
| - | [[Category: Glideosome]]
| + | |
| - | [[Category: Gliding motility]]
| + | |
| - | [[Category: Ja]]
| + | |
| - | [[Category: Jasplakinolide]]
| + | |
| - | [[Category: Malaria parasite]]
| + | |
| - | [[Category: Plasmodium]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| - | [[Category: Thin filament]]
| + | |
| Structural highlights
Function
ACT1_PLAFX 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.
Publication Abstract from PubMed
During their life cycle, apicomplexan parasites, such as the malaria parasite Plasmodium falciparum, use actomyosin-driven gliding motility to move and invade host cells. For this process, actin filament length and stability are temporally and spatially controlled. In contrast to canonical actin, P. falciparum actin 1 (PfAct1) does not readily polymerize into long, stable filaments. The structural basis of filament instability, which plays a pivotal role in host cell invasion, and thus infectivity, is poorly understood, largely because high-resolution structures of PfAct1 filaments were missing. Here, we report the near-atomic structure of jasplakinolide (JAS)-stabilized PfAct1 filaments determined by electron cryomicroscopy. The general filament architecture is similar to that of mammalian F-actin. The high resolution of the structure allowed us to identify small but important differences at inter- and intrastrand contact sites, explaining the inherent instability of apicomplexan actin filaments. JAS binds at regular intervals inside the filament to three adjacent actin subunits, reinforcing filament stability by hydrophobic interactions. Our study reveals the high-resolution structure of a small molecule bound to F-actin, highlighting the potential of electron cryomicroscopy for structure-based drug design. Furthermore, our work serves as a strong foundation for understanding the structural design and evolution of actin filaments and their function in motility and host cell invasion of apicomplexan parasites.
Near-atomic structure of jasplakinolide-stabilized malaria parasite F-actin reveals the structural basis of filament instability.,Pospich S, Kumpula EP, von der Ecken J, Vahokoski J, Kursula I, Raunser S Proc Natl Acad Sci U S A. 2017 Sep 18. pii: 201707506. doi:, 10.1073/pnas.1707506114. PMID:28923924[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Pospich S, Kumpula EP, von der Ecken J, Vahokoski J, Kursula I, Raunser S. Near-atomic structure of jasplakinolide-stabilized malaria parasite F-actin reveals the structural basis of filament instability. Proc Natl Acad Sci U S A. 2017 Sep 18. pii: 201707506. doi:, 10.1073/pnas.1707506114. PMID:28923924 doi:http://dx.doi.org/10.1073/pnas.1707506114
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