4TJV
Crystal structure of protease-associated domain of Arabidopsis vacuolar sorting receptor 1
Summary for 4TJV
| Entry DOI | 10.2210/pdb4tjv/pdb |
| Related | 4TJX |
| Descriptor | Vacuolar-sorting receptor 1, IODIDE ION (3 entities in total) |
| Functional Keywords | ligand-binding domain, beta barrel, apo form, protein transport |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Cellular location | Membrane; Single-pass type I membrane protein: P93026 |
| Total number of polymer chains | 1 |
| Total formula weight | 18592.67 |
| Authors | Luo, F.,Fong, Y.H.,Jiang, L.W.,Wong, K.B. (deposition date: 2014-05-25, release date: 2014-12-10, Last modification date: 2024-11-20) |
| Primary citation | Luo, F.,Fong, Y.H.,Zeng, Y.,Shen, J.,Jiang, L.,Wong, K.B. How vacuolar sorting receptor proteins interact with their cargo proteins: crystal structures of apo and cargo-bound forms of the protease-associated domain from an Arabidopsis vacuolar sorting receptor. Plant Cell, 26:3693-3708, 2014 Cited by PubMed Abstract: In plant cells, soluble proteins are directed to vacuoles because they contain vacuolar sorting determinants (VSDs) that are recognized by vacuolar sorting receptors (VSR). To understand how a VSR recognizes its cargo, we present the crystal structures of the protease-associated domain of VSR isoform 1 from Arabidopsis thaliana (VSR1PA) alone and complexed with a cognate peptide containing the barley (Hordeum vulgare) aleurain VSD sequence of 1ADSNPIRPVT10. The crystal structures show that VSR1PA binds the sequence, Ala-Asp-Ser, preceding the NPIR motif. A conserved cargo binding loop, with a consensus sequence of 95RGxCxF100, forms a cradle that accommodates the cargo-peptide. In particular, Arg-95 forms a hydrogen bond to the Ser-3 position of the VSD, and the essential role of Arg-95 and Ser-3 in receptor-cargo interaction was supported by a mutagenesis study. Cargo binding induces conformational changes that are propagated from the cargo binding loop to the C terminus via conserved residues in switch I-IV regions. The resulting 180° swivel motion of the C-terminal tail is stabilized by a hydrogen bond between Glu-24 and His-181. A mutagenesis study showed that these two residues are essential for cargo interaction and trafficking. Based on our structural and functional studies, we present a model of how VSRs recognize their cargos. PubMed: 25271241DOI: 10.1105/tpc.114.129940 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.651 Å) |
Structure validation
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