7abk

Helical structure of PspA

spinqualitylabelsall models 7abk, resolution 3.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.6Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed PspA is the main effector of the phage shock protein (Psp) system and preserves the bacterial inner membrane integrity and function. Here, we present the 3.6 A resolution cryoelectron microscopy (cryo-EM) structure of PspA assembled in helical rods. PspA monomers adopt a canonical ESCRT-III fold in an extended open conformation. PspA rods are capable of enclosing lipids and generating positive membrane curvature. Using cryo-EM, we visualized how PspA remodels membrane vesicles into mum-sized structures and how it mediates the formation of internalized vesicular structures. Hotspots of these activities are zones derived from PspA assemblies, serving as lipid transfer platforms and linking previously separated lipid structures. These membrane fusion and fission activities are in line with the described functional properties of bacterial PspA/IM30/LiaH proteins. Our structural and functional analyses reveal that bacterial PspA belongs to the evolutionary ancestry of ESCRT-III proteins involved in membrane remodeling. PspA adopts an ESCRT-III-like fold and remodels bacterial membranes.,Junglas B, Huber ST, Heidler T, Schlosser L, Mann D, Hennig R, Clarke M, Hellmann N, Schneider D, Sachse C Cell. 2021 Jul 8;184(14):3674-3688.e18. doi: 10.1016/j.cell.2021.05.042. Epub, 2021 Jun 23. PMID:34166616 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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