This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
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.
Get5 Carboxyl-terminal Domain Is a Novel Dimerization Motif That Tethers an Extended Get4/Get5 Complex.,Chartron JW, Vandervelde DG, Rao M, Clemons WM Jr J Biol Chem. 2012 Mar 9;287(11):8310-7. Epub 2012 Jan 17. PMID:22262836[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Chartron JW, Vandervelde DG, Rao M, Clemons WM Jr. Get5 Carboxyl-terminal Domain Is a Novel Dimerization Motif That Tethers an Extended Get4/Get5 Complex. J Biol Chem. 2012 Mar 9;287(11):8310-7. Epub 2012 Jan 17. PMID:22262836 doi:10.1074/jbc.M111.333252
