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6i7e

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Plasmodium falciparum Myosin A, Pre-powerstroke

Structural highlights

6i7e is a 1 chain structure with sequence from Plasmodium falciparum 3D7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.492Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).

Publication Abstract from PubMed

Plasmodium parasites are obligate intracellular protozoa and causative agents of malaria, responsible for half a million deaths each year. The lifecycle progression of the parasite is reliant on cell motility, a process driven by myosin A, an unconventional single-headed class XIV molecular motor. Here we demonstrate that myosin A from Plasmodium falciparum (PfMyoA) is critical for red blood cell invasion. Further, using a combination of X-ray crystallography, kinetics, and in vitro motility assays, we elucidate the non-canonical interactions that drive this motor's function. We show that PfMyoA motor properties are tuned by heavy chain phosphorylation (Ser19), with unphosphorylated PfMyoA exhibiting enhanced ensemble force generation at the expense of speed. Regulated phosphorylation may therefore optimize PfMyoA for enhanced force generation during parasite invasion or for fast motility during dissemination. The three PfMyoA crystallographic structures presented here provide a blueprint for discovery of specific inhibitors designed to prevent parasite infection.

Plasmodium myosin A drives parasite invasion by an atypical force generating mechanism.,Robert-Paganin J, Robblee JP, Auguin D, Blake TCA, Bookwalter CS, Krementsova EB, Moussaoui D, Previs MJ, Jousset G, Baum J, Trybus KM, Houdusse A Nat Commun. 2019 Jul 23;10(1):3286. doi: 10.1038/s41467-019-11120-0. PMID:31337750^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Robert-Paganin J, Robblee JP, Auguin D, Blake TCA, Bookwalter CS, Krementsova EB, Moussaoui D, Previs MJ, Jousset G, Baum J, Trybus KM, Houdusse A. Plasmodium myosin A drives parasite invasion by an atypical force generating mechanism. Nat Commun. 2019 Jul 23;10(1):3286. doi: 10.1038/s41467-019-11120-0. PMID:31337750 doi:http://dx.doi.org/10.1038/s41467-019-11120-0

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6i7e"

@@ Line 3: / Line 3: @@
 <StructureSection load='6i7e' size='340' side='right'caption='[[6i7e]], [[Resolution|resolution]] 3.49&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6i7e]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I7E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6I7E FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6i7e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_3D7 Plasmodium falciparum 3D7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I7E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6I7E 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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</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]] 3.492&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6i7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i7e OCA], [http://pdbe.org/6i7e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6i7e RCSB], [http://www.ebi.ac.uk/pdbsum/6i7e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6i7e 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=6i7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i7e OCA], [https://pdbe.org/6i7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6i7e RCSB], [https://www.ebi.ac.uk/pdbsum/6i7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6i7e ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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).
+[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 ==
@@ Line 19: / Line 19: @@
 </div>
 <div class="pdbe-citations 6i7e" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Myosin 3D Structures|Myosin 3D Structures]]
 == References ==
 <references/>
@@ Line 24: / Line 27: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Auguin, D]]
+[[Category: Plasmodium falciparum 3D7]]
-[[Category: Baum, J]]
+[[Category: Auguin D]]
-[[Category: Houdusse, A]]
+[[Category: Baum J]]
-[[Category: Jousset, G]]
+[[Category: Houdusse A]]
-[[Category: Moussaoui, D]]
+[[Category: Jousset G]]
-[[Category: Robert-Paganin, J]]
+[[Category: Moussaoui D]]
-[[Category: Trybus, K M]]
+[[Category: Robert-Paganin J]]
-[[Category: Motor protein]]
+[[Category: Trybus KM]]
-[[Category: Myosin some]]
-[[Category: Plasmodium falciparum]]
-[[Category: Tunable mechanism]]

6i7e

From Proteopedia

Current revision

Plasmodium falciparum Myosin A, Pre-powerstroke

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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