6FM2

CARP domain of mouse cyclase-associated protein 1 (CAP1) bound to ADP-actin

6FM2 の概要

• エントリーDOI: 10.2210/pdb6fm2/pdb
• 分子名称: Actin, alpha skeletal muscle, Adenylyl cyclase-associated protein 1, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: complex, actin cytoskeleton, nucleotide exchange, actin turnover, structural protein
• 由来する生物種: Mus musculus (Mouse); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton: P68135; Cell membrane ; Peripheral membrane protein : P40124
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59846.18

構造登録者

Kotila, T.M.,Kogan, K.,Lappalainen, P. (登録日: 2018-01-30, 公開日: 2018-05-16, 最終更新日: 2024-01-17)

主引用文献

Kotila, T.,Kogan, K.,Enkavi, G.,Guo, S.,Vattulainen, I.,Goode, B.L.,Lappalainen, P.
Structural basis of actin monomer re-charging by cyclase-associated protein.
Nat Commun, 9:1892-1892, 2018

PubMed Abstract: Actin polymerization powers key cellular processes, including motility, morphogenesis, and endocytosis. The actin turnover cycle depends critically on "re-charging" of ADP-actin monomers with ATP, but whether this reaction requires dedicated proteins in cells, and the underlying mechanism, have remained elusive. Here we report that nucleotide exchange catalyzed by the ubiquitous cytoskeletal regulator cyclase-associated protein (CAP) is critical for actin-based processes in vivo. We determine the structure of the CAP-actin complex, which reveals that nucleotide exchange occurs in a compact, sandwich-like complex formed between the dimeric actin-binding domain of CAP and two ADP-actin monomers. In the crystal structure, the C-terminal tail of CAP associates with the nucleotide-sensing region of actin, and this interaction is required for rapid re-charging of actin by both yeast and mammalian CAPs. These data uncover the conserved structural basis and biological role of protein-catalyzed re-charging of actin monomers.

PubMed: 29760438
DOI: 10.1038/s41467-018-04231-7

実験手法

X-RAY DIFFRACTION (2.8 Å)