9b1r | pdb_00009b1r
Functional implication of the homotrimeric multidomain vacuolar sorting receptor 1 from Arabidopsis thaliana
Structural highlights
FunctionVSR1_ARATH Vacuolar-sorting receptor (VSR) involved in clathrin-coated vesicles sorting from Golgi apparatus to vacuoles. Required for the sorting of 12S globulin, 2S albumin and maybe other seed storage proteins to protein storage vacuoles (PSVs) in seeds. May also be implicated in targeting N-terminal propeptide containing proteins to lytic vacuoles.[1] [2] Publication Abstract from PubMedThe vacuolar sorting receptors (VSRs) are specific to plants and are responsible for sorting and transporting particular proteins from the trans-Golgi network to the vacuole. This process is critically important for various cellular functions, including storing nutrients during seed development. Despite many years of intense studies on VSRs, a complete relation between function and structure has not yet been revealed. Here, we present the crystal structure of the entire luminal region of glycosylated VSR1 from Arabidopsis thaliana (AtVSR1) for the first time. The structure provides insights into the tertiary and quaternary structures of VSR1, which are composed of an N-terminal protease-associated (PA) domain, a unique central region, and one epidermal growth factor (EGF)-like domain followed by two disordered EGF-like domains. The structure of VSR1 exhibits unique characteristics, the significance of which is yet to be fully understood. Functional implication of the homotrimeric multidomain vacuolar sorting receptor 1 (VSR1) from Arabidopsis thaliana.,Park H, Youn B, Park DJ, Puthanveettil SV, Kang C Sci Rep. 2024 Apr 26;14(1):9622. doi: 10.1038/s41598-024-57975-2. PMID:38671060[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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