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| | ==Crystal structure of Plasmodium falciparum actin I== | | ==Crystal structure of Plasmodium falciparum actin I== |
| - | <StructureSection load='4cbu' size='340' side='right' caption='[[4cbu]], [[Resolution|resolution]] 1.30Å' scene=''> | + | <StructureSection load='4cbu' size='340' side='right'caption='[[4cbu]], [[Resolution|resolution]] 1.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4cbu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice] and [http://en.wikipedia.org/wiki/Plafa Plafa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CBU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4cbu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CBU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cbw|4cbw]], [[4cbx|4cbx]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=4cbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbu OCA], [http://pdbe.org/4cbu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cbu RCSB], [http://www.ebi.ac.uk/pdbsum/4cbu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cbu 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=4cbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbu OCA], [https://pdbe.org/4cbu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cbu RCSB], [https://www.ebi.ac.uk/pdbsum/4cbu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cbu 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. [[http://www.uniprot.org/uniprot/GELS_MOUSE GELS_MOUSE]] Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis. | + | [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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| | ==See Also== | | ==See Also== |
| - | *[[Actin|Actin]] | + | *[[Actin 3D structures|Actin 3D structures]] |
| - | *[[Gelsolin|Gelsolin]] | + | *[[Gelsolin 3D structures|Gelsolin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Plafa]] | + | [[Category: Mus musculus]] |
| - | [[Category: Andreadaki, M]] | + | [[Category: Plasmodium falciparum]] |
| - | [[Category: Bhargav, S P]] | + | [[Category: Andreadaki M]] |
| - | [[Category: Desfosses, A]] | + | [[Category: Bhargav SP]] |
| - | [[Category: Frischknecht, F]] | + | [[Category: Desfosses A]] |
| - | [[Category: Ignatev, A]] | + | [[Category: Frischknecht F]] |
| - | [[Category: Kumpula, E P]] | + | [[Category: Ignatev A]] |
| - | [[Category: Kursula, I]] | + | [[Category: Kumpula EP]] |
| - | [[Category: Lepper, S]] | + | [[Category: Kursula I]] |
| - | [[Category: Martinez, S Munico]] | + | [[Category: Lepper S]] |
| - | [[Category: Sachse, C]] | + | [[Category: Munico Martinez S]] |
| - | [[Category: Siden-Kiamos, I]] | + | [[Category: Sachse C]] |
| - | [[Category: Vahokoski, J]] | + | [[Category: Siden-Kiamos I]] |
| - | [[Category: Malaria]]
| + | [[Category: Vahokoski J]] |
| - | [[Category: Motility]]
| + | |
| - | [[Category: Motor protein]]
| + | |
| - | [[Category: Parasite]]
| + | |
| 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
Actins are highly conserved proteins and key players in central processes in all eukaryotic cells. The two actins of the malaria parasite are among the most divergent eukaryotic actins and also differ from each other more than isoforms in any other species. Microfilaments have not been directly observed in Plasmodium and are presumed to be short and highly dynamic. We show that actin I cannot complement actin II in male gametogenesis, suggesting critical structural differences. Cryo-EM reveals that Plasmodium actin I has a unique filament structure, whereas actin II filaments resemble canonical F-actin. Both Plasmodium actins hydrolyze ATP more efficiently than alpha-actin, and unlike any other actin, both parasite actins rapidly form short oligomers induced by ADP. Crystal structures of both isoforms pinpoint several structural changes in the monomers causing the unique polymerization properties. Inserting the canonical D-loop to Plasmodium actin I leads to the formation of long filaments in vitro. In vivo, this chimera restores gametogenesis in parasites lacking actin II, suggesting that stable filaments are required for exflagellation. Together, these data underline the divergence of eukaryotic actins and demonstrate how structural differences in the monomers translate into filaments with different properties, implying that even eukaryotic actins have faced different evolutionary pressures and followed different paths for developing their polymerization properties.
Structural differences explain diverse functions of Plasmodium actins.,Vahokoski J, Bhargav SP, Desfosses A, Andreadaki M, Kumpula EP, Martinez SM, Ignatev A, Lepper S, Frischknecht F, Siden-Kiamos I, Sachse C, Kursula I PLoS Pathog. 2014 Apr 17;10(4):e1004091. doi: 10.1371/journal.ppat.1004091., eCollection 2014 Apr. PMID:24743229[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Vahokoski J, Bhargav SP, Desfosses A, Andreadaki M, Kumpula EP, Martinez SM, Ignatev A, Lepper S, Frischknecht F, Siden-Kiamos I, Sachse C, Kursula I. Structural differences explain diverse functions of Plasmodium actins. PLoS Pathog. 2014 Apr 17;10(4):e1004091. doi: 10.1371/journal.ppat.1004091., eCollection 2014 Apr. PMID:24743229 doi:http://dx.doi.org/10.1371/journal.ppat.1004091
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