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.
3ug7 is a 4 chain structure with sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Efficient delivery of membrane proteins is a critical cellular process. The recently elucidated GET (Guided Entry of TA proteins) pathway is responsible for the targeted delivery of tail-anchored (TA) membrane proteins to the endoplasmic reticulum. The central player is the ATPase Get3, which in its free form exists as a dimer. Biochemical evidence suggests a role for a tetramer of Get3. Here, we present the first crystal structure of an archaeal Get3 homologue that exists as a tetramer and is capable of TA protein binding. The tetramer generates a hydrophobic chamber that we propose binds the TA protein. We use small-angle X-ray scattering to provide the first structural information of a fungal Get3/TA protein complex showing that the overall molecular envelope is consistent with the archaeal tetramer structure. Moreover, we show that this fungal tetramer complex is capable of TA insertion. This allows us to suggest a model where a tetramer of Get3 sequesters a TA protein during targeting to the membrane.
Tail-anchor targeting by a Get3 tetramer: the structure of an archaeal homologue.,Suloway CJ, Rome ME, Clemons WM Jr EMBO J. 2011 Nov 29. doi: 10.1038/emboj.2011.433. PMID:22124326[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Suloway CJ, Rome ME, Clemons WM Jr. Tail-anchor targeting by a Get3 tetramer: the structure of an archaeal homologue. EMBO J. 2011 Nov 29. doi: 10.1038/emboj.2011.433. PMID:22124326 doi:10.1038/emboj.2011.433
