1PFZ
PROPLASMEPSIN II FROM PLASMODIUM FALCIPARUM
Summary for 1PFZ
| Entry DOI | 10.2210/pdb1pfz/pdb |
| Descriptor | PROPLASMEPSIN II, GLYCEROL (3 entities in total) |
| Functional Keywords | aspartic proteinase zymogen, hemoglobinase, malaria, hydrolase, aspartyl protease, glycoprotein, aspartic protease zymogen |
| Biological source | Plasmodium falciparum (malaria parasite P. falciparum) |
| Cellular location | Vacuole: P46925 |
| Total number of polymer chains | 4 |
| Total formula weight | 171485.91 |
| Authors | Bernstein, N.K.,Cherney, M.M.,Loetscher, H.,Ridley, R.G.,James, M.N.G. (deposition date: 1998-07-07, release date: 1999-01-13, Last modification date: 2024-11-06) |
| Primary citation | Bernstein, N.K.,Cherney, M.M.,Loetscher, H.,Ridley, R.G.,James, M.N. Crystal structure of the novel aspartic proteinase zymogen proplasmepsin II from plasmodium falciparum. Nat.Struct.Biol., 6:32-37, 1999 Cited by 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. PubMed: 9886289DOI: 10.1038/4905 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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