2LNZ
Solution structure of the Get5 carboxyl domain from S. cerevisiae
2LNZ の概要
エントリーDOI | 10.2210/pdb2lnz/pdb |
関連するPDBエントリー | 2LO0 3VEJ |
NMR情報 | BMRB: 18186 |
分子名称 | Ubiquitin-like protein MDY2 (1 entity in total) |
機能のキーワード | dimerization, homodimerization, protein binding |
由来する生物種 | Saccharomyces cerevisiae (Baker's yeast) |
細胞内の位置 | Cytoplasm, cytosol: Q12285 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 14247.78 |
構造登録者 | Chartron, J.W.,Vandervelde, D.G.,Rao, M.,Clemons Jr., W.M. (登録日: 2012-01-08, 公開日: 2012-01-25, 最終更新日: 2024-05-15) |
主引用文献 | 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 主引用文献が同じPDBエントリー |
実験手法 | SOLUTION NMR |
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