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3VEJ

Crystal structure of the Get5 carboxyl domain from S. cerevisiae

Summary for 3VEJ
Entry DOI10.2210/pdb3vej/pdb
Related2LNZ 2LO0
DescriptorUbiquitin-like protein MDY2, PHOSPHATE ION (3 entities in total)
Functional Keywordsalpha helical, dimerization, homodimerization, protein binding
Biological sourceSaccharomyces cerevisiae (Baker's yeast)
Cellular locationCytoplasm, cytosol: Q12285
Total number of polymer chains2
Total formula weight9563.62
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: 2024-02-28)
Primary citationChartron, 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: 22262836
DOI: 10.1074/jbc.M111.333252
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.23 Å)
Structure validation

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