3MN6

Structures of actin-bound WH2 domains of Spire and the implication for filament nucleation

3MN6 の概要

• エントリーDOI: 10.2210/pdb3mn6/pdb
• 関連するPDBエントリー: 2HF4 3MMV 3MN5 3MN7 3MN9
• 分子名称: Actin-5C, Protein spire, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: wh2 domain, spire, actin complex, contractile protein-protein binding complex, contractile protein/protein binding
• 由来する生物種: Drosophila melanogaster (Fruit fly); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton: P10987 Q9U1K1
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 131717.38

構造登録者

Ducka, A.M.,Sitar, T.,Popowicz, G.M.,Huber, R.,Holak, T.A. (登録日: 2010-04-21, 公開日: 2010-06-02, 最終更新日: 2023-09-06)

主引用文献

Ducka, A.M.,Joel, P.,Popowicz, G.M.,Trybus, K.M.,Schleicher, M.,Noegel, A.A.,Huber, R.,Holak, T.A.,Sitar, T.
Structures of actin-bound Wiskott-Aldrich syndrome protein homology 2 (WH2) domains of Spire and the implication for filament nucleation.
Proc.Natl.Acad.Sci.USA, 107:11757-11762, 2010

PubMed Abstract: Three classes of proteins are known to nucleate new filaments: the Arp2/3 complex, formins, and the third group of proteins that contain ca. 25 amino acid long actin-binding Wiskott-Aldrich syndrome protein homology 2 domains, called the WH2 repeats. Crystal structures of the complexes between the actin-binding WH2 repeats of the Spire protein and actin were determined for the Spire single WH2 domain D, the double (SpirCD), triple (SpirBCD), quadruple (SpirABCD) domains, and an artificial Spire WH2 construct comprising three identical D repeats (SpirDDD). SpirCD represents the minimal functional core of Spire that can nucleate actin filaments. Packing in the crystals of the actin complexes with SpirCD, SpirBCD, SpirABCD, and SpirDDD shows the presence of two types of assemblies, "side-to-side" and "straight-longitudinal," which can serve as actin filament nuclei. The principal feature of these structures is their loose, open conformations, in which the sides of actins that normally constitute the inner interface core of a filament are flipped inside out. These Spire structures are distant from those seen in the filamentous nuclei of Arp2/3, formins, and in the F-actin filament.

PubMed: 20538977
DOI: 10.1073/pnas.1005347107

実験手法

X-RAY DIFFRACTION (2 Å)