1U5T
Structure of the ESCRT-II endosomal trafficking complex
Summary for 1U5T
| Entry DOI | 10.2210/pdb1u5t/pdb |
| Descriptor | appears to be functionally related to SNF7; Snf8p, Defective in vacuolar protein sorting; Vps36p, Hypothetical 23.6 kDa protein in YUH1-URA8 intergenic region (3 entities in total) |
| Functional Keywords | escrt, endosomal, trafficking, protein complex, transport protein |
| Biological source | Saccharomyces cerevisiae (baker's yeast) More |
| Cellular location | Cytoplasm: Q12483 Q06696 P47142 |
| Total number of polymer chains | 4 |
| Total formula weight | 93811.00 |
| Authors | Hierro, A.,Sun, J.,Rusnak, A.S.,Kim, J.,Prag, G.,Emr, S.D.,Hurley, J.H. (deposition date: 2004-07-28, release date: 2004-09-21, Last modification date: 2024-02-14) |
| Primary citation | Hierro, A.,Sun, J.,Rusnak, A.S.,Kim, J.,Prag, G.,Emr, S.D.,Hurley, J.H. Structure of ESCRT-II endosomal trafficking complex Nature, 431:221-225, 2004 Cited by PubMed Abstract: The multivesicular-body (MVB) pathway delivers transmembrane proteins and lipids to the lumen of the endosome. The multivesicular-body sorting pathway has crucial roles in growth-factor-receptor downregulation, developmental signalling, regulation of the immune response and the budding of certain enveloped viruses such as human immunodeficiency virus. Ubiquitination is a signal for sorting into the MVB pathway, which also requires the functions of three protein complexes, termed ESCRT-I, -II and -III (endosomal sorting complex required for transport). Here we report the crystal structure of the core of the yeast ESCRT-II complex, which contains one molecule of the Vps protein Vps22, the carboxy-terminal domain of Vps36 and two molecules of Vps25, and has the shape of a capital letter 'Y'. The amino-terminal coiled coil of Vps22 and the flexible linker leading to the ubiquitin-binding NZF domain of Vps36 both protrude from the tip of one branch of the 'Y'. Vps22 and Vps36 form nearly equivalent interactions with the two Vps25 molecules at the centre of the 'Y'. The structure suggests how ubiquitinated cargo could be passed between ESCRT components of the MVB pathway through the sequential transfer of ubiquitinated cargo from one complex to the next. PubMed: 15329733DOI: 10.1038/nature02914 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.6 Å) |
Structure validation
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