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==Structure of the Plasmodium MTIP-MyoA complex, a key component of the parasite invasion motor== | |||
<StructureSection load='2auc' size='340' side='right'caption='[[2auc]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
| | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2auc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_knowlesi Plasmodium knowlesi] and [https://en.wikipedia.org/wiki/Plasmodium_yoelii_yoelii Plasmodium yoelii yoelii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AUC 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]] 2.6Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SAC:N-ACETYL-SERINE'>SAC</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=2auc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2auc OCA], [https://pdbe.org/2auc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2auc RCSB], [https://www.ebi.ac.uk/pdbsum/2auc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2auc ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/D0VWV5_PLAKN D0VWV5_PLAKN] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
== | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/au/2auc_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2auc ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The causative agents of malaria have developed a sophisticated machinery for entering multiple cell types in the human and insect hosts. In this machinery, a critical interaction occurs between the unusual myosin motor MyoA and the MyoA-tail Interacting Protein (MTIP). Here we present one crystal structure that shows three different conformations of Plasmodium MTIP, one of these in complex with the MyoA-tail, which reveal major conformational changes in the C-terminal domain of MTIP upon binding the MyoA-tail helix, thereby creating several hydrophobic pockets in MTIP that are the recipients of key hydrophobic side chains of MyoA. Because we also show that the MyoA helix is able to block parasite growth, this provides avenues for designing antimalarials. | The causative agents of malaria have developed a sophisticated machinery for entering multiple cell types in the human and insect hosts. In this machinery, a critical interaction occurs between the unusual myosin motor MyoA and the MyoA-tail Interacting Protein (MTIP). Here we present one crystal structure that shows three different conformations of Plasmodium MTIP, one of these in complex with the MyoA-tail, which reveal major conformational changes in the C-terminal domain of MTIP upon binding the MyoA-tail helix, thereby creating several hydrophobic pockets in MTIP that are the recipients of key hydrophobic side chains of MyoA. Because we also show that the MyoA helix is able to block parasite growth, this provides avenues for designing antimalarials. | ||
Structure of the MTIP-MyoA complex, a key component of the malaria parasite invasion motor.,Bosch J, Turley S, Daly TM, Bogh SM, Villasmil ML, Roach C, Zhou N, Morrisey JM, Vaidya AB, Bergman LW, Hol WG Proc Natl Acad Sci U S A. 2006 Mar 28;103(13):4852-7. Epub 2006 Mar 17. PMID:16547135<ref>PMID:16547135</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2auc" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Plasmodium knowlesi]] | [[Category: Plasmodium knowlesi]] | ||
[[Category: | [[Category: Plasmodium yoelii yoelii]] | ||
[[Category: Bosch | [[Category: Bosch J]] | ||
[[Category: Hol | [[Category: Hol WGJ]] | ||
[[Category: Turley S]] | |||
[[Category: Turley | |||
Latest revision as of 14:18, 22 May 2024
Structure of the Plasmodium MTIP-MyoA complex, a key component of the parasite invasion motorStructure of the Plasmodium MTIP-MyoA complex, a key component of the parasite invasion motor
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe causative agents of malaria have developed a sophisticated machinery for entering multiple cell types in the human and insect hosts. In this machinery, a critical interaction occurs between the unusual myosin motor MyoA and the MyoA-tail Interacting Protein (MTIP). Here we present one crystal structure that shows three different conformations of Plasmodium MTIP, one of these in complex with the MyoA-tail, which reveal major conformational changes in the C-terminal domain of MTIP upon binding the MyoA-tail helix, thereby creating several hydrophobic pockets in MTIP that are the recipients of key hydrophobic side chains of MyoA. Because we also show that the MyoA helix is able to block parasite growth, this provides avenues for designing antimalarials. Structure of the MTIP-MyoA complex, a key component of the malaria parasite invasion motor.,Bosch J, Turley S, Daly TM, Bogh SM, Villasmil ML, Roach C, Zhou N, Morrisey JM, Vaidya AB, Bergman LW, Hol WG Proc Natl Acad Sci U S A. 2006 Mar 28;103(13):4852-7. Epub 2006 Mar 17. PMID:16547135[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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