4lvo

Crystal structure of PfSUB1-prodomain-NIMP.M7 Fab complex with added CaCl2

spinqualitylabelsall models 4lvo, resolution 2.26Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4lvo is a 4 chain structure with sequence from Mus musculus and Plasmodium falciparum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.26Å Ligands: CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SUB1_PLAFA Serine protease which plays an essential role in merozoite invasion of and egress from host erythrocytes by processing and activating various merozoite surface and parasitophorous vacuole proteins. Mediates the proteolytic maturation of serine proteases SERA4, SERA5 and SERA6 just prior to merozoite egress. Prior to merozoite egress, cleaves merozoite surface proteins MSP1, MSP6 and MSP7, which form the MSP1/6/7 complex, and thereby may prime the parasite cell surface for invasion of fresh erythrocytes. Prior to merozoite egress, cleaves MSRP2 converting it to MSRP2 p25 form, and RAP1 converting it to RAP1 p67 form.[UniProtKB:Q8I0V0] Publication Abstract from PubMed 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 A, 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. The malaria parasite egress protease SUB1 is a calcium-dependent redox switch subtilisin.,Withers-Martinez C, Strath M, Hackett F, Haire LF, Howell SA, Walker PA, Evangelos C, Dodson GG, Blackman MJ Nat Commun. 2014 May 2;5:3726. doi: 10.1038/ncomms4726. PMID:24785947 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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