9fp8 | pdb_00009fp8

Crystal structure of Anopheles gambiae actin depolymerizing factor

spinqualitylabelsall models 9fp8, resolution 1.68Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9fp8 is a 2 chain structure with sequence from Anopheles gambiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.68Å Ligands: GOL, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0NGL9_ANOGA Publication Abstract from PubMed Actin is an intrinsically dynamic protein, the function and state of which are modulated by actin-binding proteins. Actin-depolymerizing factors (ADF)/cofilins are ubiquitous actin-binding proteins that accelerate actin turnover. Malaria is an infectious disease caused by parasites of the genus Plasmodium, which belong to the phylum Apicomplexa. The parasites require two hosts to complete their life cycle: the definitive host, or the vector, an Anopheles spp. mosquito, and a vertebrate intermediate host, such as humans. Here, the malaria vector Anopheles gambiae ADF (AgADF) crystal structure is reported. AgADF has a conserved ADF/cofilin fold with six central beta-strands surrounded by five alpha-helices with a long beta-hairpin loop protruding out of the structure. The G- and F-actin-binding sites of AgADF are conserved, and the structure shows features of potential importance for regulation by membrane binding and redox state. AgADF binds monomeric ATP- and ADP-actin with a high affinity, having a nanomolar K(d), and binds effectively also to actin filaments. Crystal structure of Anopheles gambiae actin depolymerizing factor explains high affinity to monomeric actin.,Lasiwa D, Kursula I FEBS J. 2025 Feb 11. doi: 10.1111/febs.70007. PMID:39932036 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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