4tjx | pdb_00004tjx

Crystal structure of protease-associated domain of Arabidopsis VSR1 in complex with aleurain peptide

spinqualitylabelsall models 4tjx, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4tjx is a 2 chain structure with sequence from Arabidopsis thaliana and Hordeum vulgare. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.902Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function VSR1_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. Publication Abstract from PubMed 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 degrees 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. 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.,Luo F, Fong YH, Zeng Y, Shen J, Jiang L, Wong KB Plant Cell. 2014 Sep;26(9):3693-708. doi: 10.1105/tpc.114.129940. Epub 2014 Sep, 30. PMID:25271241 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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