2ZIH
Crystal Structure of Yeast Vps74
Summary for 2ZIH
| Entry DOI | 10.2210/pdb2zih/pdb |
| Related | 2ZII |
| Descriptor | Vacuolar protein sorting-associated protein 74 (2 entities in total) |
| Functional Keywords | beta hairpin, vps, golgi localization, vps74, tetramer, golgi apparatus, phosphoprotein, protein transport, transport |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Golgi apparatus, Golgi stack membrane ; Peripheral membrane protein ; Cytoplasmic side : Q06385 |
| Total number of polymer chains | 4 |
| Total formula weight | 157915.50 |
| Authors | Schmitz, K.R.,Li, S.,Setty, T.G.,Ferguson, K.M. (deposition date: 2008-02-18, release date: 2008-04-22, Last modification date: 2024-03-13) |
| Primary citation | Schmitz, K.R.,Liu, J.,Li, S.,Setty, T.G.,Wood, C.S.,Burd, C.G.,Ferguson, K.M. Golgi localization of glycosyltransferases requires a Vps74p oligomer. Dev.Cell, 14:523-534, 2008 Cited by PubMed Abstract: The mechanism of glycosyltransferase localization to the Golgi apparatus is a long-standing question in secretory cell biology. All Golgi glycosyltransferases are type II membrane proteins with small cytosolic domains that contribute to Golgi localization. To date, no protein has been identified that recognizes the cytosolic domains of Golgi enzymes and contributes to their localization. Here, we report that yeast Vps74p directly binds to the cytosolic domains of cis and medial Golgi mannosyltransferases and that loss of this interaction correlates with loss of Golgi localization of these enzymes. We have solved the X-ray crystal structure of Vps74p and find that it forms a tetramer, which we also observe in solution. Deletion of a critical structural motif disrupts tetramer formation and results in loss of Vps74p localization and function. Vps74p is highly homologous to the human GMx33 Golgi matrix proteins, suggesting a conserved function for these proteins in the Golgi enzyme localization machinery. PubMed: 18410729DOI: 10.1016/j.devcel.2008.02.016 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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