4d60
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Structure of a dimeric Plasmodium falciparum profilin mutant== | |
+ | <StructureSection load='4d60' size='340' side='right'caption='[[4d60]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4d60]] is a 16 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=4D60 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D60 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]] 3.3Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4d60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d60 OCA], [https://pdbe.org/4d60 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d60 RCSB], [https://www.ebi.ac.uk/pdbsum/4d60 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d60 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/PROF_PLAF7 PROF_PLAF7] 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 (By similarity).[UniProtKB:P86294] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Gene fusion is a common mechanism of protein evolution that has mainly been discussed in the context of multidomain or symmetric proteins. Less is known about fusion of ancestral genes to produce small single-domain proteins. Here, we show with a domain-swapped mutant Plasmodium profilin that this small, globular, apparently single-domain protein consists of two foldons. The separation of binding sites for different protein ligands in the two halves suggests evolution via an ancient gene fusion event, analogous to the formation of multidomain proteins. Finally, the two fragments can be assembled together after expression as two separate gene products. The possibility to engineer both domain-swapped dimers and half-profilins that can be assembled back to a full profilin provides perspectives for engineering of novel protein folds, e.g., with different scaffolding functions. | ||
- | + | Two independently folding units of Plasmodium profilin suggest evolution via gene fusion.,Bhargav SP, Vahokoski J, Kallio JP, Torda AE, Kursula P, Kursula I Cell Mol Life Sci. 2015 May 27. PMID:26012696<ref>PMID:26012696</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
- | [[Category: | + | <div class="pdbe-citations 4d60" style="background-color:#fffaf0;"></div> |
- | [[Category: | + | |
- | [[Category: | + | ==See Also== |
- | [[Category: Kursula | + | *[[Profilin 3D Structures|Profilin 3D Structures]] |
- | [[Category: Torda | + | == References == |
- | [[Category: | + | <references/> |
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Plasmodium falciparum]] | ||
+ | [[Category: Bhargav SP]] | ||
+ | [[Category: Kallio JP]] | ||
+ | [[Category: Kursula I]] | ||
+ | [[Category: Kursula P]] | ||
+ | [[Category: Torda A]] | ||
+ | [[Category: Vahokoski J]] |
Current revision
Structure of a dimeric Plasmodium falciparum profilin mutant
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