6ycx: Difference between revisions
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The | ==Plasmodium falciparum Myosin A full-length, pre-powerstroke state== | ||
<StructureSection load='6ycx' size='340' side='right'caption='[[6ycx]], [[Resolution|resolution]] 3.99Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ycx]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_3D7 Plasmodium falciparum 3D7] and [https://en.wikipedia.org/wiki/Plasmodium_falciparum_NF54 Plasmodium falciparum NF54]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YCX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YCX FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.99Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</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=6ycx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ycx OCA], [https://pdbe.org/6ycx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ycx RCSB], [https://www.ebi.ac.uk/pdbsum/6ycx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ycx ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MYOA_PLAF7 MYOA_PLAF7] Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Parasites from the genus Plasmodium are the causative agents of malaria. The mobility, infectivity, and ultimately pathogenesis of Plasmodium falciparum rely on a macromolecular complex, called the glideosome. At the core of the glideosome is an essential and divergent Myosin A motor (PfMyoA), a first order drug target against malaria. Here, we present the full-length structure of PfMyoA in two states of its motor cycle. We report novel interactions that are essential for motor priming and the mode of recognition of its two light chains (PfELC and MTIP) by two degenerate IQ motifs. Kinetic and motility assays using PfMyoA variants, along with molecular dynamics, demonstrate how specific priming and atypical sequence adaptations tune the motor's mechano-chemical properties. Supported by evidence for an essential role of the PfELC in malaria pathogenesis, these structures provide a blueprint for the design of future anti-malarials targeting both the glideosome motor and its regulatory elements. | |||
Full-length Plasmodium falciparum myosin A and essential light chain PfELC structures provide new anti-malarial targets.,Moussaoui D, Robblee JP, Auguin D, Krementsova EB, Haase S, Blake TCA, Baum J, Robert-Paganin J, Trybus KM, Houdusse A Elife. 2020 Oct 13;9:e60581. doi: 10.7554/eLife.60581. PMID:33046215<ref>PMID:33046215</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6ycx" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Myosin 3D Structures|Myosin 3D Structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Plasmodium falciparum 3D7]] | |||
[[Category: Plasmodium falciparum NF54]] | |||
[[Category: Auguin D]] | |||
[[Category: Houdusse A]] | |||
[[Category: Krementsova EB]] | |||
[[Category: Moussaoui D]] | |||
[[Category: Robblee JP]] | |||
[[Category: Robert-Paganin J]] | |||
[[Category: Trybus KM]] | |||
Latest revision as of 16:24, 24 January 2024
Plasmodium falciparum Myosin A full-length, pre-powerstroke statePlasmodium falciparum Myosin A full-length, pre-powerstroke state
Structural highlights
FunctionMYOA_PLAF7 Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity). Publication Abstract from PubMedParasites from the genus Plasmodium are the causative agents of malaria. The mobility, infectivity, and ultimately pathogenesis of Plasmodium falciparum rely on a macromolecular complex, called the glideosome. At the core of the glideosome is an essential and divergent Myosin A motor (PfMyoA), a first order drug target against malaria. Here, we present the full-length structure of PfMyoA in two states of its motor cycle. We report novel interactions that are essential for motor priming and the mode of recognition of its two light chains (PfELC and MTIP) by two degenerate IQ motifs. Kinetic and motility assays using PfMyoA variants, along with molecular dynamics, demonstrate how specific priming and atypical sequence adaptations tune the motor's mechano-chemical properties. Supported by evidence for an essential role of the PfELC in malaria pathogenesis, these structures provide a blueprint for the design of future anti-malarials targeting both the glideosome motor and its regulatory elements. Full-length Plasmodium falciparum myosin A and essential light chain PfELC structures provide new anti-malarial targets.,Moussaoui D, Robblee JP, Auguin D, Krementsova EB, Haase S, Blake TCA, Baum J, Robert-Paganin J, Trybus KM, Houdusse A Elife. 2020 Oct 13;9:e60581. doi: 10.7554/eLife.60581. PMID:33046215[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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