2WOJ

ADP-AlF4 complex of S. cerevisiae GET3

2WOJ の概要

• エントリーDOI: 10.2210/pdb2woj/pdb
• 分子名称: ATPASE GET3, ADENOSINE-5'-DIPHOSPHATE, TETRAFLUOROALUMINATE ION, ... (6 entities in total)
• 機能のキーワード: tail-anchored, membrane protein, targeting factor, endoplasmic reticulum, get3, atpase, trc40, atp-binding, golgi apparatus, er-golgi transport, nucleotide-binding, arsenical resistance, nucleus, hydrolase, cytoplasm, transport, arsa, arsenite
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• 細胞内の位置: Cytoplasm: Q12154
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 159923.10

構造登録者

Mateja, A.,Szlachcic, A.,Downing, M.E.,Dobosz, M.,Mariappan, M.,Hegde, R.S.,Keenan, R.J. (登録日: 2009-07-26, 公開日: 2009-08-11, 最終更新日: 2024-05-01)

主引用文献

Mateja, A.,Szlachcic, A.,Downing, M.E.,Dobosz, M.,Mariappan, M.,Hegde, R.S.,Keenan, R.J.
The Structural Basis of Tail-Anchored Membrane Protein Recognition by Get3.
Nature, 461:361-, 2009

PubMed Abstract: Targeting of newly synthesized membrane proteins to the endoplasmic reticulum is an essential cellular process. Most membrane proteins are recognized and targeted co-translationally by the signal recognition particle. However, nearly 5% of membrane proteins are 'tail-anchored' by a single carboxy-terminal transmembrane domain that cannot access the co-translational pathway. Instead, tail-anchored proteins are targeted post-translationally by a conserved ATPase termed Get3. The mechanistic basis for tail-anchored protein recognition or targeting by Get3 is not known. Here we present crystal structures of yeast Get3 in 'open' (nucleotide-free) and 'closed' (ADP.AlF(4)(-)-bound) dimer states. In the closed state, the dimer interface of Get3 contains an enormous hydrophobic groove implicated by mutational analyses in tail-anchored protein binding. In the open state, Get3 undergoes a striking rearrangement that disrupts the groove and shields its hydrophobic surfaces. These data provide a molecular mechanism for nucleotide-regulated binding and release of tail-anchored proteins during their membrane targeting by Get3.

PubMed: 19675567
DOI: 10.1038/NATURE08319

実験手法

X-RAY DIFFRACTION (1.994 Å)