2Q36

Actin Dimer Cross-linked between Residues 191 and 374 and complexed with Kabiramide C

2Q36 の概要

• エントリーDOI: 10.2210/pdb2q36/pdb
• 関連するPDBエントリー: 1QZ5 2Q31
• 分子名称: Actin, alpha skeletal muscle, CALCIUM ION, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: cross-linked dimer, structural 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: 43548.13

構造登録者

Sawaya, M.R.,Pashkov, I.,Kudryashov, D.S.,Reisler, E.,Yeates, T.O. (登録日: 2007-05-29, 公開日: 2007-06-05, 最終更新日: 2023-08-30)

主引用文献

Sawaya, M.R.,Kudryashov, D.S.,Pashkov, I.,Adisetiyo, H.,Reisler, E.,Yeates, T.O.
Multiple crystal structures of actin dimers and their implications for interactions in the actin filament.
Acta Crystallogr.,Sect.D, 64:454-465, 2008

PubMed Abstract: The structure of actin in its monomeric form is known at high resolution, while the structure of filamentous F-actin is only understood at considerably lower resolution. Knowing precisely how the monomers of actin fit together would lead to a deeper understanding of the dynamic behavior of the actin filament. Here, a series of crystal structures of actin dimers are reported which were prepared by cross-linking in either the longitudinal or the lateral direction in the filament state. Laterally cross-linked dimers, comprised of monomers belonging to different protofilaments, are found to adopt configurations in crystals that are not related to the native structure of filamentous actin. In contrast, multiple structures of longitudinal dimers consistently reveal the same interface between monomers within a single protofilament. The reappearance of the same longitudinal interface in multiple crystal structures adds weight to arguments that the interface visualized is similar to that in actin filaments. Highly conserved atomic interactions involving residues 199-205 and 287-291 are highlighted.

PubMed: 18391412
DOI: 10.1107/S0907444908003351

実験手法

X-RAY DIFFRACTION (2.5 Å)