4ZKD

Crystal structure of the S. cerevisiae Ski7 GTPase-like domain, bound to GDP and inorganic phosphate.

4ZKD の概要

• エントリーDOI: 10.2210/pdb4zkd/pdb
• 分子名称: Superkiller protein 7, PHOSPHATE ION, GUANOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: gtpase, translation, ngd, ski, hydrolase, gtp-binding protein
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• 細胞内の位置: Cytoplasm : Q08491
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 57220.95

構造登録者

Kowalinski, E.,Conti, E. (登録日: 2015-04-30, 公開日: 2015-06-17, 最終更新日: 2024-05-08)

主引用文献

Kowalinski, E.,Schuller, A.,Green, R.,Conti, E.
Saccharomyces cerevisiae Ski7 Is a GTP-Binding Protein Adopting the Characteristic Conformation of Active Translational GTPases.
Structure, 23:1336-1343, 2015

PubMed Abstract: Ski7 is a cofactor of the cytoplasmic exosome in budding yeast, functioning in both mRNA turnover and non-stop decay (NSD), a surveillance pathway that degrades faulty mRNAs lacking a stop codon. The C-terminal region of Ski7 (Ski7C) shares overall sequence similarity with the translational GTPase (trGTPase) Hbs1, but whether Ski7 has retained the properties of a trGTPase is unclear. Here, we report the high-resolution structures of Ski7C bound to either intact guanosine triphosphate (GTP) or guanosine diphosphate-Pi. The individual domains of Ski7C adopt the conformation characteristic of active trGTPases. Furthermore, the nucleotide-binding site of Ski7C shares similar features compared with active trGTPases, notably the presence of a characteristic monovalent cation. However, a suboptimal polar residue at the putative catalytic site and an unusual polar residue that interacts with the γ-phosphate of GTP distinguish Ski7 from other trGTPases, suggesting it might function rather as a GTP-binding protein than as a GTP-hydrolyzing enzyme.

PubMed: 26051716
DOI: 10.1016/j.str.2015.04.018

実験手法

X-RAY DIFFRACTION (2.181 Å)