7eqx

Crystal structure of an Aedes aegypti procarboxypeptidase B1

spinqualitylabelsall models 7eqx, resolution 2.08Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7eqx is a 4 chain structure with sequence from Aedes aegypti. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.08Å Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1S4F020_AEDAE Publication Abstract from PubMed Metallocarboxypeptidases play critical roles in the development of mosquitoes and influence pathogen/parasite infection of the mosquito midgut. Here, we report the crystal structure of Aedes aegypti procarboxypeptidase B1 (PCPBAe1), characterized its substrate specificity and mechanism of binding to and inhibiting Dengue virus (DENV). We show that the activated PCPBAe1 (CPBAe1) hydrolyzes both Arg- and Lys-substrates, which is modulated by residues Asp(251) and Ser(239) Notably, these residues are conserved in CPBs across mosquito species, possibly required for efficient digestion of basic dietary residues that are necessary for mosquito reproduction and development. Importantly, we characterized the interaction between PCPBAe1 and DENV envelope (E) protein, virus-like particles, and infectious virions. We identified residues Asp(18A), Glu(19A), Glu(85), Arg(87), and Arg(89) of PCPBAe1 are essential for interaction with DENV. PCPBAe1 maps to the dimeric interface of the E protein domains I/II (Lys(64)-Glu(84), Val(238)-Val(252), and Leu(278)-Leu(287)). Overall, our studies provide general insights into how the substrate-binding property of mosquito carboxypeptidases could be targeted to potentially control mosquito populations or proposes a mechanism by which PCPBAe1 binds to and inhibits DENV. Structure of Aedes aegypti procarboxypeptidase B1 and its binding with Dengue virus for controlling infection.,Gavor E, Choong YK, Tulsian NK, Nayak D, Idris F, Sivaraman H, Ting DHR, Sylvie A, Mok YK, Kini RM, Sivaraman J Life Sci Alliance. 2021 Nov 8;5(1):e202101211. doi: 10.26508/lsa.202101211. Print , 2022 Jan. PMID:34750241 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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