6abs

Actin interacting protein 5 (Aip5, mutant)

spinqualitylabelsall models 6abs, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6abs is a 2 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: 1PE, PGE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function YFI6_YEAST Publication Abstract from PubMed A multiprotein complex polarisome nucleates actin cables for polarized cell growth in budding yeast and filamentous fungi. However, the dynamic regulations of polarisome proteins in polymerizing actin under physiological and stress conditions remains unknown. We identify a previously functionally unknown polarisome member, actin-interacting-protein 5 (Aip5), which promotes actin assembly synergistically with formin Bni1. Aip5-C terminus is responsible for its activities by interacting with G-actin and Bni1. Through N-terminal intrinsically disordered region, Aip5 forms high-order oligomers and generate cytoplasmic condensates under the stresses conditions. The molecular dynamics and reversibility of Aip5 condensates are regulated by scaffolding protein Spa2 via liquid-liquid phase separation both in vitro and in vivo. In the absence of Spa2, Aip5 condensates hamper cell growth and actin cable structures under stress treatment. The present study reveals the mechanisms of actin assembly for polarity establishment and the adaptation in stress conditions to protect actin assembly by protein phase separation. Polarisome scaffolder Spa2-mediated macromolecular condensation of Aip5 for actin polymerization.,Xie Y, Sun J, Han X, Tursic-Wunder A, Toh JDW, Hong W, Gao YG, Miao Y Nat Commun. 2019 Nov 7;10(1):5078. doi: 10.1038/s41467-019-13125-1. PMID:31699995 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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