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< | ==Plasmodium falciparum profilin== | ||
<StructureSection load='2jkf' size='340' side='right'caption='[[2jkf]], [[Resolution|resolution]] 2.31Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2jkf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JKF 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]] 2.31Å</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=2jkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jkf OCA], [https://pdbe.org/2jkf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jkf RCSB], [https://www.ebi.ac.uk/pdbsum/2jkf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jkf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PROF_PLAFX PROF_PLAFX] Essential for the invasive blood stages of the parasite. Binds to proline rich sequences in various regulatory formin-like proteins and also to membrane phospholipids. Binds to actin and affects the structure of the cytoskeleton. Weakly sequesters actin monomers.<ref>PMID:19000816</ref> | |||
== 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/jk/2jkf_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=2jkf ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Profilins are key regulators of actin dynamics. They sequester actin monomers, forming a pool for rapid polymer formation stimulated by proteins such as formins. Apicomplexan parasites utilize a highly specialized microfilament system for motility and host cell invasion. Their genomes encode only a small number of divergent actin regulators. We present the first crystal structure of an apicomplexan profilin, that of the malaria parasite Plasmodium falciparum, alone and in complex with a polyproline ligand peptide. The most striking feature of Plasmodium profilin is a unique minidomain consisting of a large beta-hairpin extension common to all apicomplexan parasites, and an acidic loop specific for Plasmodium species. Reverse genetics in the rodent malaria model, Plasmodium berghei, suggests that profilin is essential for the invasive blood stages of the parasite. Together, our data establish the structural basis for understanding the functions of profilin in the malaria parasite. | |||
Structural basis for parasite-specific functions of the divergent profilin of Plasmodium falciparum.,Kursula I, Kursula P, Ganter M, Panjikar S, Matuschewski K, Schuler H Structure. 2008 Nov 12;16(11):1638-48. PMID:19000816<ref>PMID:19000816</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2jkf" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Profilin 3D Structures|Profilin 3D Structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
== | |||
[[Category: | |||
[[Category: Plasmodium falciparum]] | [[Category: Plasmodium falciparum]] | ||
[[Category: | [[Category: Ganter M]] | ||
[[Category: | [[Category: Kursula I]] | ||
[[Category: | [[Category: Kursula P]] | ||
[[Category: Matuschewski K]] | |||
[[Category: Panjikar S]] | |||
[[Category: Schueler H]] | |||
Latest revision as of 12:38, 9 May 2024
Plasmodium falciparum profilinPlasmodium falciparum profilin
Structural highlights
FunctionPROF_PLAFX Essential for the invasive blood stages of the parasite. Binds to proline rich sequences in various regulatory formin-like proteins and also to membrane phospholipids. Binds to actin and affects the structure of the cytoskeleton. Weakly sequesters actin monomers.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedProfilins are key regulators of actin dynamics. They sequester actin monomers, forming a pool for rapid polymer formation stimulated by proteins such as formins. Apicomplexan parasites utilize a highly specialized microfilament system for motility and host cell invasion. Their genomes encode only a small number of divergent actin regulators. We present the first crystal structure of an apicomplexan profilin, that of the malaria parasite Plasmodium falciparum, alone and in complex with a polyproline ligand peptide. The most striking feature of Plasmodium profilin is a unique minidomain consisting of a large beta-hairpin extension common to all apicomplexan parasites, and an acidic loop specific for Plasmodium species. Reverse genetics in the rodent malaria model, Plasmodium berghei, suggests that profilin is essential for the invasive blood stages of the parasite. Together, our data establish the structural basis for understanding the functions of profilin in the malaria parasite. Structural basis for parasite-specific functions of the divergent profilin of Plasmodium falciparum.,Kursula I, Kursula P, Ganter M, Panjikar S, Matuschewski K, Schuler H Structure. 2008 Nov 12;16(11):1638-48. PMID:19000816[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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