The malaria parasite egress protease SUB1 is a calcium-dependent redox switch subtilisin View Full Text


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Article Info

DATE

2014-12

AUTHORS

Chrislaine Withers-Martinez, Malcolm Strath, Fiona Hackett, Lesley F. Haire, Steven A. Howell, Philip A. Walker, Evangelos Christodoulou, Guy G. Dodson, Michael J. Blackman

ABSTRACT

Malaria is caused by a protozoan parasite that replicates within an intraerythrocytic parasitophorous vacuole. Release (egress) of malaria merozoites from the host erythrocyte is a highly regulated and calcium-dependent event that is critical for disease progression. Minutes before egress, an essential parasite serine protease called SUB1 is discharged into the parasitophorous vacuole, where it proteolytically processes a subset of parasite proteins that play indispensable roles in egress and invasion. Here we report the first crystallographic structure of Plasmodium falciparum SUB1 at 2.25 Å, in complex with its cognate prodomain. The structure highlights the basis of the calcium dependence of SUB1, as well as its unusual requirement for interactions with substrate residues on both prime and non-prime sides of the scissile bond. Importantly, the structure also reveals the presence of a solvent-exposed redox-sensitive disulphide bridge, unique among the subtilisin family, that likely acts as a regulator of protease activity in the parasite. More... »

PAGES

3726

References to SciGraph publications

  • 2008. Protein Structure Modeling with MODELLER in STRUCTURAL PROTEOMICS
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/ncomms4726

    DOI

    http://dx.doi.org/10.1038/ncomms4726

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1017880531

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/24785947


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