9yqq | pdb_00009yqq

Cryo-EM structure of the VPS13C C-terminal region

spinqualitylabelsall models 9yqq, resolution 3.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9yqq is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.8Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease VP13C_HUMAN Young-onset Parkinson disease. The disease is caused by variants affecting the gene represented in this entry. Function VP13C_HUMAN Mediates the transfer of lipids between membranes at organelle contact sites (By similarity). Necessary for proper mitochondrial function and maintenance of mitochondrial transmembrane potential (PubMed:26942284). Involved in the regulation of PINK1/PRKN-mediated mitophagy in response to mitochondrial depolarization (PubMed:26942284).[UniProtKB:Q07878] Publication Abstract from PubMed Bridge-like lipid transfer proteins (BLTPs) play central roles in redistributing lipids from their primary site of synthesis in the endoplasmic reticulum to other organelles. They comprise bridge-domains spanning between organelles at contact sites that allow lipids to transit the cytosol between adjacent membranes. The assembly of BLTPs into complexes with adaptor proteins enables their lipid transfer ability. To address the mechanisms underlying assembly and regulation of BLTP complexes, we used cryo-EM to resolve the structure of one such BLTP, the Parkinson's protein VPS13C, at near-atomic resolution. The structure identifies a lipid-transfer-nonpermissive conformation, where the built-in C-terminal VAB adaptor module blocks the end of the lipid transfer bridge, interfering with lipid delivery. We also identify calmodulin, central to calcium signaling, as a VPS13 partner, suggesting calcium regulation of VPS13 function. Altogether, this structure of intact VPS13C serves as starting point to understand its regulation and, more broadly, that of other BLTPs. Insights into the regulation of VPS13 family bridge-like lipid transfer proteins from the structure of VPS13C.,Li D, Wang X, Hu B, Hao H, Hamill S, Li Y, Chen G, De Camilli P, Reinisch KM bioRxiv [Preprint]. 2025 Nov 11:2025.11.10.687702. doi: , 10.1101/2025.11.10.687702. PMID:41292763 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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