Solution NMR structure of a sheddase inhibitor prodomain from the malarial parasite Plasmodium falciparum.

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TitleSolution NMR structure of a sheddase inhibitor prodomain from the malarial parasite Plasmodium falciparum.
Publication TypeJournal Article
Year of Publication2012
AuthorsHe, Y, Chen, Y, Oganesyan, N, Ruan, B, O'Brochta, DA, Bryan, PN, Orban, J
JournalProteins
Volume80
Issue12
Pagination2810-7
Date Published2012 Dec
ISSN1097-0134
KeywordsAmino Acid Sequence, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Plasmodium falciparum, Protein Structure, Tertiary, Sequence Alignment, Solutions, Subtilisins
Abstract

Plasmodium subtilisin 2 (Sub2) is a multidomain protein that plays an important role in malaria infection. Here, we describe the solution NMR structure of a conserved region of the inhibitory prodomain of Sub2 from Plasmodium falciparum, termed prosub2. Despite the absence of any detectable sequence homology, the protozoan prosub2 has structural similarity to bacterial and mammalian subtilisin-like prodomains. Comparison with the three-dimensional structures of these other prodomains suggests a likely binding interface with the catalytic domain of Sub2 and provides insights into the locations of primary and secondary processing sites in Plasmodium prodomains.

DOI10.1002/prot.24187
Alternate JournalProteins
PubMed ID23011838