4TJX

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

Summary for 4TJX

• Entry DOI: 10.2210/pdb4tjx/pdb
• Related: 4TJV
• Descriptor: Vacuolar-sorting receptor 1, Aleurain peptide (3 entities in total)
• Functional Keywords: complex structure, ligand-binding domain, aleurain pepetide, beta-barrel, protein transport
• Biological source: Arabidopsis thaliana (Mouse-ear cress); More
• Cellular location: Membrane; Single-pass type I membrane protein: P93026
• Total number of polymer chains: 2
• Total formula weight: 18901.42

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

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: 25271241
DOI: 10.1105/tpc.114.129940

Experimental method

X-RAY DIFFRACTION (1.902 Å)