Crystal structure of the novel aspartic proteinase zymogen proplasmepsin II from plasmodium falciparum.
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Bernstein NK, Cherney MM, Loetscher H, Ridley RG, James MN
Crystal structure of the novel aspartic proteinase zymogen proplasmepsin II from plasmodium falciparum.
Nat Struct Biol. 1999 Jan;6(1):32-7.
- PubMed ID
- 9886289 [ View in PubMed]
- Abstract
Proplasmepsin II is the zymogen of plasmepsin II, an aspartic proteinase used by Plasmodiumfalciparum to digest hemoglobin during the blood stage of malaria. A large shift between the N-domain and the central and C-domains of proplasmepsin II opens the active site cleft, preventing the formation of a functional aspartic proteinase active site. This mode of inhibition of catalytic activity has not been observed in any other aspartic proteinase zymogen. Instead of occluding a pre-formed active site, as in the gastric aspartic proteinase zymogens, the prosegment of proplasmepsin II interacts extensively with the C-domain and serves as a 'harness' to keep the domains apart. Disruption of key salt bridges at low pH may be important in activation.