Summary for 7U6F
| Entry DOI | 10.2210/pdb7u6f/pdb |
| EMDB information | 24964 |
| Descriptor | Vacuolar protein sorting-associated protein 35, Vacuolar protein sorting-associated protein 26A, Vacuolar protein sorting-associated protein 29, ... (7 entities in total) |
| Functional Keywords | retromer, membrane trafficking, endosomal trafficking, membrane coat complexes, protein transport, transport protein |
| Biological source | Mus musculus (house mouse) More |
| Total number of polymer chains | 3 |
| Total formula weight | 152531.23 |
| Authors | Kendall, A.K.,Chandra, M.,Jackson, L.P. (deposition date: 2022-03-04, release date: 2022-10-12, Last modification date: 2024-06-12) |
| Primary citation | Kendall, A.K.,Chandra, M.,Xie, B.,Wan, W.,Jackson, L.P. Improved mammalian retromer cryo-EM structures reveal a new assembly interface. J.Biol.Chem., 298:102523-102523, 2022 Cited by PubMed Abstract: Retromer (VPS26/VPS35/VPS29 subunits) assembles with multiple sorting nexin proteins on membranes to mediate endosomal recycling of transmembrane protein cargoes. Retromer has been implicated in other cellular processes, including mitochondrial homeostasis, nutrient sensing, autophagy, and fission events. Mechanisms for mammalian retromer assembly remain undefined, and retromer engages multiple sorting nexin proteins to sort cargoes to different destinations. Published structures demonstrate mammalian retromer forms oligomers in vitro, but several structures were poorly resolved. We report here improved retromer oligomer structures using single-particle cryo-EM by combining data collected from tilted specimens with multiple advancements in data processing, including using a 3D starting model for enhanced automated particle picking in RELION. We used a retromer mutant (3KE retromer) that breaks VPS35-mediated interfaces to determine a structure of a new assembly interface formed by the VPS26A and VPS35 N-termini. The interface reveals how an N-terminal VPS26A arrestin saddle can link retromer chains by engaging a neighboring VPS35 N- terminus, on the opposite side from the well-characterized C-VPS26/N-VPS35 interaction observed within heterotrimers. The new interaction interface exhibits substantial buried surface area (∼7000 Å) and further suggests that metazoan retromer may serve as an adaptable scaffold. PubMed: 36174678DOI: 10.1016/j.jbc.2022.102523 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.9 Å) |
Structure validation
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