7zty

Structure of Vps39 N-terminal domain from Chaetomium thermophilum

spinqualitylabelsall models 7zty, resolution 2.89Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7zty is a 1 chain structure with sequence from Chaetomium thermophilum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.89Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G0RY05_CHATD Publication Abstract from PubMed Lysosomes are essential for cellular recycling, nutrient signaling, autophagy, and pathogenic bacteria and viruses invasion. Lysosomal fusion is fundamental to cell survival and requires HOPS, a conserved heterohexameric tethering complex. On the membranes to be fused, HOPS binds small membrane-associated GTPases and assembles SNAREs for fusion, but how the complex fulfills its function remained speculative. Here, we used cryo-electron microscopy to reveal the structure of HOPS. Unlike previously reported, significant flexibility of HOPS is confined to its extremities, where GTPase binding occurs. The SNARE-binding module is firmly attached to the core, therefore, ideally positioned between the membranes to catalyze fusion. Our data suggest a model for how HOPS fulfills its dual functionality of tethering and fusion and indicate why it is an essential part of the membrane fusion machinery. Structure of the HOPS tethering complex, a lysosomal membrane fusion machinery.,Shvarev D, Schoppe J, Konig C, Perz A, Fullbrunn N, Kiontke S, Langemeyer L, Januliene D, Schnelle K, Kummel D, Frohlich F, Moeller A, Ungermann C Elife. 2022 Sep 13;11:e80901. doi: 10.7554/eLife.80901. PMID:36098503 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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