3R3Q
Crystal structure of the yeast Vps23 UEV domain
Summary for 3R3Q
| Entry DOI | 10.2210/pdb3r3q/pdb |
| Related | 3R42 |
| Descriptor | Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease, ZINC ION, CHLORIDE ION, ... (6 entities in total) |
| Functional Keywords | endosomal sorting, escrt-i, protein transport |
| Biological source | Saccharomyces cerevisiae (yeast) |
| Cellular location | Cytoplasm: P25604 |
| Total number of polymer chains | 1 |
| Total formula weight | 19353.44 |
| Authors | Ren, X.,Hurley, J.H. (deposition date: 2011-03-16, 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 Cited by 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: 21505419DOI: 10.1038/emboj.2011.122 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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