4GOC
Crystal structure of the Get5 ubiquitin-like domain
Summary for 4GOC
| Entry DOI | 10.2210/pdb4goc/pdb |
| Related | 4GOD 4GOE 4GOF |
| Descriptor | Golgi to ER traffic protein 5 (2 entities in total) |
| Functional Keywords | ubiquitin-like domain, protein-protein interaction, sgt2, protein binding |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Cellular location | Cytoplasm, cytosol: Q12285 |
| Total number of polymer chains | 3 |
| Total formula weight | 25632.03 |
| Authors | Chartron, J.W.,VanderVelde, D.G.,Clemons Jr., W.M. (deposition date: 2012-08-19, release date: 2012-11-21, Last modification date: 2024-02-28) |
| Primary citation | Chartron, J.W.,Vandervelde, D.G.,Clemons, W.M. Structures of the Sgt2/SGTA Dimerization Domain with the Get5/UBL4A UBL Domain Reveal an Interaction that Forms a Conserved Dynamic Interface. Cell Rep, 2:1620-1632, 2012 Cited by PubMed Abstract: In the cytoplasm, the correct delivery of membrane proteins is an essential and highly regulated process. The posttranslational targeting of the important tail-anchor membrane (TA) proteins has recently been under intense investigation. A specialized pathway, called the guided entry of TA proteins (GET) pathway in yeast and the transmembrane domain recognition complex (TRC) pathway in vertebrates, recognizes endoplasmic-reticulum-targeted TA proteins and delivers them through a complex series of handoffs. An early step is the formation of a complex between Sgt2/SGTA, a cochaperone with a presumed ubiquitin-like-binding domain (UBD), and Get5/UBL4A, a ubiquitin-like domain (UBL)-containing protein. We structurally characterize this UBD/UBL interaction for both yeast and human proteins. This characterization is supported by biophysical studies that demonstrate that complex formation is mediated by electrostatics, generating an interface that has high-affinity with rapid kinetics. In total, this work provides a refined model of the interplay of Sgt2 homologs in TA targeting. PubMed: 23142665DOI: 10.1016/j.celrep.2012.10.010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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