9bl8

MIT (L7C/A43C) Domain of Vps4p

spinqualitylabelsall models 9bl8, resolution 1.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9bl8 is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.3Å Ligands: CL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function VPS4_YEAST Involved in the transport of biosynthetic membrane proteins from the prevacuolar/endosomal compartment to the vacuole. Required for multivesicular body (MVB) protein sorting. Catalyzes the ATP-dependent dissociation of class E VPS proteins from endosomal membranes, such as the disassembly of the ESCRT-III complex. Publication Abstract from PubMed The ESCRT pathway's AAA+ ATPase, Vps4p, remodels ESCRT-III complexes to drive membrane fission. Here, we use peptide binding assays to further the understanding of substrate specificity and the mechanism of autoinhibition. Our results reveal unexpected sequence preference to the substrate binding groove and an elegant mechanism of regulation that couples localization to substrate with release from autoinhibition. Vps4 substrate binding and coupled mechanisms of Vps4p substrate recruitment and release from autoinhibition.,Wienkers HJ, Han H, Whitby FG, Hill CP bioRxiv [Preprint]. 2024 Sep 7:2024.09.07.611824. doi: 10.1101/2024.09.07.611824. PMID:39282404 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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