3R42

Crystal structure of the yeast vps23 UEV domain in complex with a vps27 PSDP peptide

Summary for 3R42

• Entry DOI: 10.2210/pdb3r42/pdb
• Related: 3R3Q
• Descriptor: Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease, Vacuolar protein sorting-associated protein 27 (3 entities in total)
• Functional Keywords: endosomal sorting, escrt, protein transport
• Biological source: Saccharomyces cerevisiae (yeast); More
• Cellular location: Cytoplasm: P25604; Endosome membrane; Peripheral membrane protein; Cytoplasmic side: P40343
• Total number of polymer chains: 2
• Total formula weight: 19091.65

Authors

Ren, X.,Hurley, J.H. (deposition date: 2011-03-17, release date: 2011-05-04, Last modification date: 2023-09-13)

Primary citation

Ren, X.,Hurley, J.H.
Structural basis for endosomal recruitment of ESCRT-I by ESCRT-0 in yeast.
Embo J., 30:2130-2139, 2011

PubMed Abstract: The ESCRT-0 and ESCRT-I complexes coordinate the clustering of ubiquitinated cargo with intralumenal budding of the endosomal membrane, two essential steps in vacuolar/lysosomal protein sorting from yeast to humans. The 1.85-Å crystal structure of interacting regions of the yeast ESCRT-0 and ESCRT-I complexes reveals that PSDP motifs of the Vps27 ESCRT-0 subunit bind to a novel electropositive N-terminal site on the UEV domain of the ESCRT-I subunit Vps23 centred on Trp16. This novel site is completely different from the C-terminal part of the human UEV domain that binds to P(S/T)AP motifs of human ESCRT-0 and HIV-1 Gag. Disruption of the novel PSDP-binding site eliminates the interaction in vitro and blocks enrichment of Vps23 in endosome-related class E compartments in yeast cells. However, this site is non-essential for sorting of the ESCRT cargo Cps1. Taken together, these results show how a conserved motif/domain pair can evolve to use strikingly different binding modes in different organisms.

PubMed: 21505419
DOI: 10.1038/emboj.2011.122

Experimental method

X-RAY DIFFRACTION (1.866 Å)