4tr2 | pdb_00004tr2

Crystal structure of PvSUB1

spinqualitylabelsall models 4tr2, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4tr2 is a 2 chain structure with sequence from Plasmodium vivax. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: CA, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function E6Y8B9_PLAVI Publication Abstract from PubMed The Plasmodium subtilase SUB1 plays a pivotal role during the egress of malaria parasites from host hepatocytes and erythrocytes. Here we report the crystal structure of full-length SUB1 from the human-infecting parasite Plasmodium vivax, revealing a bacterial-like catalytic domain in complex with a Plasmodium-specific prodomain. The latter displays a novel architecture with an amino-terminal insertion that functions as a 'belt', embracing the catalytic domain to further stabilize the quaternary structure of the pre-protease, and undergoes calcium-dependent autoprocessing during subsequent activation. Although dispensable for recombinant enzymatic activity, the SUB1 'belt' could not be deleted in Plasmodium berghei, suggesting an essential role of this domain for parasite development in vivo. The SUB1 structure not only provides a valuable platform to develop new anti-malarial candidates against this promising drug target, but also defines the Plasmodium-specific 'belt' domain as a key calcium-dependent regulator of SUB1 during parasite egress from host cells. A novel Plasmodium-specific prodomain fold regulates the malaria drug target SUB1 subtilase.,Giganti D, Bouillon A, Tawk L, Robert F, Martinez M, Crublet E, Weber P, Girard-Blanc C, Petres S, Haouz A, Hernandez JF, Mercereau-Puijalon O, Alzari PM, Barale JC Nat Commun. 2014 Sep 10;5:4833. doi: 10.1038/ncomms5833. PMID:25204226 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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