4d60
From Proteopedia
Structure of a dimeric Plasmodium falciparum profilin mutant
Structural highlights
FunctionPROF_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] Publication Abstract from PubMedGene 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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