6i4l: Difference between revisions
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==Crystal Structure of Plasmodium falciparum actin I (G115A mutant) in the Mg-K-ATP/ADP state== | |||
<StructureSection load='6i4l' size='340' side='right'caption='[[6i4l]], [[Resolution|resolution]] 1.83Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6i4l]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I4L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6I4L FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6i4d|6i4d]], [[6i4e|6i4e]], [[6i4f|6i4f]], [[6i4g|6i4g]], [[6i4h|6i4h]], [[6i4i|6i4i]], [[6i4j|6i4j]], [[6i4k|6i4k]]</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=6i4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i4l OCA], [http://pdbe.org/6i4l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6i4l RCSB], [http://www.ebi.ac.uk/pdbsum/6i4l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6i4l ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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. [[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. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Plasmodium actins form very short filaments and have a noncanonical link between ATP hydrolysis and polymerization. Long filaments are detrimental to the parasites, but the structural factors constraining Plasmodium microfilament lengths have remained unknown. Using high-resolution crystallography, we show that magnesium binding causes a slight flattening of the Plasmodium actin I monomer, and subsequent phosphate release results in a more twisted conformation. Thus, the Mg-bound monomer is closer in conformation to filamentous (F) actin than the Ca form, and this likely facilitates polymerization. A coordinated potassium ion resides in the active site during hydrolysis and leaves together with the phosphate, a process governed by the position of the Arg178/Asp180-containing A loop. Asp180 interacts with either Lys270 or His74, depending on the protonation state of the histidine, while Arg178 links the inner and outer domains (ID and OD) of the actin protomer. Hence, the A loop acts as a switch between stable and unstable filament conformations, the latter leading to fragmentation. Our data provide a comprehensive model for polymerization, ATP hydrolysis and phosphate release, and fragmentation of parasite microfilaments. Similar mechanisms may well exist in canonical actins, although fragmentation is much less favorable due to several subtle sequence differences as well as the methylation of His73, which is absent on the corresponding His74 in Plasmodium actin I. | |||
Atomic view into Plasmodium actin polymerization, ATP hydrolysis, and fragmentation.,Kumpula EP, Lopez AJ, Tajedin L, Han H, Kursula I PLoS Biol. 2019 Jun 14;17(6):e3000315. doi: 10.1371/journal.pbio.3000315. PMID:31199804<ref>PMID:31199804</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6i4l" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Han, H]] | |||
[[Category: Kumpula, E P]] | |||
[[Category: Kursula, I]] | [[Category: Kursula, I]] | ||
[[Category: Lopez, A J]] | |||
[[Category: Lopez, A | |||
[[Category: Tajedin, L]] | [[Category: Tajedin, L]] | ||
[[Category: Contractile protein]] | |||
[[Category: Cytoskeleton]] | |||
[[Category: Filamentous]] | |||
[[Category: Glideosome]] | |||
[[Category: Hydrolase]] | |||
Revision as of 09:50, 26 June 2019
Crystal Structure of Plasmodium falciparum actin I (G115A mutant) in the Mg-K-ATP/ADP stateCrystal Structure of Plasmodium falciparum actin I (G115A mutant) in the Mg-K-ATP/ADP state
Structural highlights
Function[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. [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. Publication Abstract from PubMedPlasmodium actins form very short filaments and have a noncanonical link between ATP hydrolysis and polymerization. Long filaments are detrimental to the parasites, but the structural factors constraining Plasmodium microfilament lengths have remained unknown. Using high-resolution crystallography, we show that magnesium binding causes a slight flattening of the Plasmodium actin I monomer, and subsequent phosphate release results in a more twisted conformation. Thus, the Mg-bound monomer is closer in conformation to filamentous (F) actin than the Ca form, and this likely facilitates polymerization. A coordinated potassium ion resides in the active site during hydrolysis and leaves together with the phosphate, a process governed by the position of the Arg178/Asp180-containing A loop. Asp180 interacts with either Lys270 or His74, depending on the protonation state of the histidine, while Arg178 links the inner and outer domains (ID and OD) of the actin protomer. Hence, the A loop acts as a switch between stable and unstable filament conformations, the latter leading to fragmentation. Our data provide a comprehensive model for polymerization, ATP hydrolysis and phosphate release, and fragmentation of parasite microfilaments. Similar mechanisms may well exist in canonical actins, although fragmentation is much less favorable due to several subtle sequence differences as well as the methylation of His73, which is absent on the corresponding His74 in Plasmodium actin I. Atomic view into Plasmodium actin polymerization, ATP hydrolysis, and fragmentation.,Kumpula EP, Lopez AJ, Tajedin L, Han H, Kursula I PLoS Biol. 2019 Jun 14;17(6):e3000315. doi: 10.1371/journal.pbio.3000315. PMID:31199804[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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