4D60

Structure of a dimeric Plasmodium falciparum profilin mutant

Summary for 4D60

• Entry DOI: 10.2210/pdb4d60/pdb
• Descriptor: PROFILIN, SULFATE ION (2 entities in total)
• Functional Keywords: structural protein, actin binding, domain swapping
• Biological source: Plasmodium falciparum
• Cellular location: Cytoplasm, cytoskeleton : P86294
• Total number of polymer chains: 16
• Total formula weight: 300859.48

Authors

Bhargav, S.P.,Vahokoski, J.,Kallio, J.P.,Torda, A.,Kursula, P.,Kursula, I. (deposition date: 2014-11-07, release date: 2015-06-03, Last modification date: 2023-12-20)

Primary citation

Bhargav, S.P.,Vahokoski, J.,Kallio, J.P.,Torda, A.E.,Kursula, P.,Kursula, I.
Two Independently Folding Units of Plasmodium Profilin Suggest Evolution Via Gene Fusion.
Cell.Mol.Life Sci., 72:4193-, 2015

PubMed Abstract: 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.

PubMed: 26012696
DOI: 10.1007/S00018-015-1932-0

Experimental method

X-RAY DIFFRACTION (3.3 Å)