3A37

Structural insight into the membrane insertion of tail-anchored proteins by Get3

3A37 の概要

• エントリーDOI: 10.2210/pdb3a37/pdb
• 関連するPDBエントリー: 3A36
• 分子名称: ATPase GET3, ADENOSINE-5'-DIPHOSPHATE, ZINC ION (3 entities in total)
• 機能のキーワード: homo dimer, atpase, zinc binding, arsenical resistance, atp-binding, cytoplasm, endoplasmic reticulum, er-golgi transport, golgi apparatus, hydrolase, nucleotide-binding, transport
• 由来する生物種: Saccharomyces cerevisiae (yeast)
• 細胞内の位置: Cytoplasm: Q12154
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 81965.34

構造登録者

Yamagata, A.,Mimura, H.,Sato, Y.,Yamashita, M.,Yoshikawa, A.,Fukai, S. (登録日: 2009-06-10, 公開日: 2010-01-12, 最終更新日: 2024-03-13)

主引用文献

Yamagata, A.,Mimura, H.,Sato, Y.,Yamashita, M.,Yoshikawa, A.,Fukai, S.
Structural insight into the membrane insertion of tail-anchored proteins by Get3
Genes Cells, 15:29-41, 2010

PubMed Abstract: Tail anchored (TA) proteins, which are important for numerous cellular processes, are defined by a single transmembrane domain (TMD) near the C-terminus. The membrane insertion of TA proteins is mediated by the highly conserved ATPase Get3. Here we report the crystal structures of Get3 in ADP-bound and nucleotide-free forms at 3.0 A and 2.8 A resolutions, respectively. Get3 consists of a nucleotide binding domain and a helical domain. Both structures exhibit a Zn(2+)-mediated homodimer in a head-to-head orientation, representing an open dimer conformation. Our cross-link experiments indicated the closed dimer-stimulating ATP hydrolysis, which might be coupled with TA-protein release. Further, our coexpression-based binding assays using a model TA protein Sec22p revealed the direct interaction between the helical domain of Get3 and the Sec22p TMD. This interaction is independent of ATP and dimer formation. Finally, we propose a structural mechanism that links ATP hydrolysis with the TA-protein insertion mediated by the conserved DTAPTGH motif.

PubMed: 20015340
DOI: 10.1111/j.1365-2443.2009.01362.x

実験手法

X-RAY DIFFRACTION (3 Å)