2A5X

Crystal Structure of a Cross-linked Actin Dimer

2A5X の概要

• エントリーDOI: 10.2210/pdb2a5x/pdb
• 分子名称: Actin, alpha skeletal muscle, CALCIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (7 entities in total)
• 機能のキーワード: muscle protein, nucleotide-binding, structural protein, contractile protein
• 由来する生物種: Oryctolagus cuniculus (rabbit)
• 細胞内の位置: Cytoplasm, cytoskeleton: P68135
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43289.12

構造登録者

Kudryashov, D.S.,Sawaya, M.R.,Adisetiyo, H.,Norcross, T.,Hegyi, G.,Reisler, E.,Yeates, T.O. (登録日: 2005-07-01, 公開日: 2005-08-23, 最終更新日: 2023-08-23)

主引用文献

Kudryashov, D.S.,Sawaya, M.R.,Adisetiyo, H.,Norcross, T.,Hegyi, G.,Reisler, E.,Yeates, T.O.
The crystal structure of a cross-linked actin dimer suggests a detailed molecular interface in F-actin
Proc.Natl.Acad.Sci.Usa, 102:13105-13110, 2005

PubMed Abstract: The 2.5-A resolution crystal structure is reported for an actin dimer, composed of two protomers cross-linked along the longitudinal (or vertical) direction of the F-actin filament. The crystal structure provides an atomic resolution view of a molecular interface between actin protomers, which we argue represents a near-native interaction in the F-actin filament. The interaction involves subdomains 3 and 4 from distinct protomers. The atomic positions in the interface visualized differ by 5-10 A from those suggested by previous models of F-actin. Such differences fall within the range of uncertainties allowed by the fiber diffraction and electron microscopy methods on which previous models have been based. In the crystal, the translational arrangement of protomers lacks the slow twist found in native filaments. A plausible model of F-actin can be constructed by reintroducing the known filament twist, without disturbing significantly the interface observed in the actin dimer crystal.

PubMed: 16141336
DOI: 10.1073/pnas.0506429102

実験手法

X-RAY DIFFRACTION (2.49 Å)