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

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...

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Bibliographic Details
Published in:Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2012-12, Vol.80 (12), p.2810-2817
Main Authors: He, Yanan, Chen, Yihong, Oganesyan, Natalia, Ruan, Biao, O'Brochta, David, Bryan, Philip N., Orban, John
Format: Article
Language:English
Subjects:
Amino Acid Sequence
malaria
Models, Molecular
Molecular Sequence Data
NMR
Nuclear Magnetic Resonance, Biomolecular - methods
Plasmodium
Plasmodium falciparum
Plasmodium falciparum - chemistry
prodomain
protease
Protein Structure, Tertiary
Sequence Alignment
sheddase
Solutions
structure
subtilisin
Subtilisins - chemistry
therapeutics
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Summary: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. Proteins 2012;. © 2012 Wiley Periodicals, Inc.
ISSN:0887-3585
1097-0134
DOI:10.1002/prot.24187