2PQR

Crystal structure of yeast Fis1 complexed with a fragment of yeast Caf4

2PQR の概要

• エントリーDOI: 10.2210/pdb2pqr/pdb
• 関連するPDBエントリー: 2PQN
• 分子名称: Mitochondria fission 1 protein, WD repeat protein YKR036C, GOLD ION, ... (4 entities in total)
• 機能のキーワード: tpr domain, protein-protein complex, apoptosis
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• 細胞内の位置: Mitochondrion outer membrane ; Single-pass membrane protein : P40515; Mitochondrion outer membrane ; Peripheral membrane protein ; Cytoplasmic side : P36130
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 44946.44

構造登録者

Zhang, Y.,Chan, D.C. (登録日: 2007-05-02, 公開日: 2007-11-06, 最終更新日: 2023-08-30)

主引用文献

Zhang, Y.,Chan, D.C.
Structural basis for recruitment of mitochondrial fission complexes by Fis1.
Proc.Natl.Acad.Sci.USA, 104:18526-18530, 2007

PubMed Abstract: Mitochondrial fission controls mitochondrial shape and physiology, including mitochondrial remodeling in apoptosis. During assembly of the yeast mitochondrial fission complex, the outer membrane protein Fis1 recruits the dynamin-related GTPase Dnm1 to mitochondria. Fis1 contains a tetratricopeptide repeat (TPR) domain and interacts with Dnm1 via the molecular adaptors Mdv1 and Caf4. By using crystallographic analysis of adaptor-Fis1 complexes, we show that these adaptors use two helices to bind to both the concave and convex surfaces of the Fis1 TPR domain. Fis1 therefore contains two interaction interfaces, a binding mode that, to our knowledge, has not been observed previously for TPR domains. Genetic and biochemical studies indicate that both binding interfaces are important for binding of Mdv1 and Caf4 to Fis1 and for mitochondrial fission activity in vivo. Our results reveal how Fis1 recruits the mitochondrial fission complex and will facilitate efforts to manipulate mitochondrial fission.

PubMed: 17998537
DOI: 10.1073/pnas.0706441104

実験手法

X-RAY DIFFRACTION (1.88 Å)