2LO0
Solution structure of the Get5 carboxyl domain from A. fumigatus
Summary for 2LO0
| Entry DOI | 10.2210/pdb2lo0/pdb |
| Related | 2lnz 3VEJ |
| NMR Information | BMRB: 18187 |
| Descriptor | Uncharacterized protein (1 entity in total) |
| Functional Keywords | dimerization, homodimerization, protein binding |
| Biological source | Aspergillus fumigatus |
| Total number of polymer chains | 2 |
| Total formula weight | 16516.06 |
| Authors | Chartron, J.W.,Vandervelde, D.G.,Rao, M.,Clemons Jr., W.M. (deposition date: 2012-01-08, release date: 2012-01-25, Last modification date: 2024-05-15) |
| Primary citation | Chartron, J.W.,Vandervelde, D.G.,Rao, M.,Clemons, W.M. Get5 Carboxyl-terminal Domain Is a Novel Dimerization Motif That Tethers an Extended Get4/Get5 Complex. J.Biol.Chem., 287:8310-8317, 2012 Cited by PubMed Abstract: Tail-anchored trans-membrane proteins are targeted to membranes post-translationally. The proteins Get4 and Get5 form an obligate complex that catalyzes the transfer of tail-anchored proteins destined to the endoplasmic reticulum from Sgt2 to the cytosolic targeting factor Get3. Get5 forms a homodimer mediated by its carboxyl domain. We show here that a conserved motif exists within the carboxyl domain. A high resolution crystal structure and solution NMR structures of this motif reveal a novel and stable helical dimerization domain. We additionally determined a solution NMR structure of a divergent fungal homolog, and comparison of these structures allows annotation of specific stabilizing interactions. Using solution x-ray scattering and the structures of all folded domains, we present a model of the full-length Get4/Get5 complex. PubMed: 22262836DOI: 10.1074/jbc.M111.333252 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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