9oj2 | pdb_00009oj2

sx20S complex (NSF-alphaSNAP-syntaxin-1a), non-hydrolyzing, class 1

spinqualitylabelsall models 9oj2, resolution 3.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9oj2 is a 14 chain structure with sequence from Cricetulus griseus and Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.75Å Ligands: ADP, ATP, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SNAA_RAT Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus. Publication Abstract from PubMed Synaptic vesicles containing neurotransmitters fuse with the plasma membrane upon the arrival of an action potential at the active zone. Multiple proteins organize trans-SNARE complex assembly and priming, leading to fusion. One target membrane SNARE, syntaxin, forms nanodomains at the active zone, and another, SNAP-25, enters non-fusogenic complexes with it. Here, we reveal mechanistic details of AAA+ protein NSF (N-ethylmaleimide sensitive factor) and SNAP (soluble NSF attachment protein) action before fusion. We show that syntaxin clusters are conserved, that NSF colocalizes with them, and characterize SNARE populations that may exist within or near them using cryo-EM. Supercomplexes of NSF, alpha-SNAP, and either a syntaxin tetramer or one of two binary complexes of syntaxin-SNAP-25 reveal atomic details of SNARE processing and show how sequential ATP hydrolysis drives disassembly. These results suggest a functional role for syntaxin clusters as reservoirs and a corresponding role for NSF in syntaxin liberation and SNARE protein quality control preceding fusion. Structural remodeling of target-SNARE protein complexes by NSF enables synaptic transmission.,White KI, Khan YA, Qiu K, Balaji A, Couoh-Cardel S, Esquivies L, Pfuetzner RA, Diao J, Brunger AT Nat Commun. 2025 Sep 24;16(1):8371. doi: 10.1038/s41467-025-62764-0. PMID:40993127 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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