8ORD

Cryo-EM map of zebrafish cardiac F-actin

8ORD の概要

• エントリーDOI: 10.2210/pdb8ord/pdb
• EMDBエントリー: 15901 17120
• 分子名称: Actin, alpha 1b, skeletal muscle, ADENOSINE-5'-DIPHOSPHATE, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: f-actin, actin, cardiac actin, filamentous, contractile protein
• 由来する生物種: Danio rerio (zebrafish)
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 212720.30

構造登録者

Bradshaw, M.,Squire, J.M.,Morris, E.,Atkinson, G.,Richardson, B.,Lees, J.,Paul, D.M. (登録日: 2023-04-13, 公開日: 2023-08-02, 最終更新日: 2023-10-11)

主引用文献

Bradshaw, M.,Squire, J.M.,Morris, E.,Atkinson, G.,Richardson, R.,Lees, J.,Caputo, M.,Bigotti, G.M.,Paul, D.M.
Zebrafish as a model for cardiac disease; Cryo-EM structure of native cardiac thin filaments from Danio Rerio.
J.Muscle Res.Cell.Motil., 44:179-192, 2023

PubMed Abstract: Actin, tropomyosin and troponin, the proteins that comprise the contractile apparatus of the cardiac thin filament, are highly conserved across species. We have used cryo-EM to study the three-dimensional structure of the zebrafish cardiac thin and actin filaments. With 70% of human genes having an obvious zebrafish orthologue, and conservation of 85% of disease-causing genes, zebrafish are a good animal model for the study of human disease. Our structure of the zebrafish thin filament reveals the molecular interactions between the constituent proteins, showing that the fundamental organisation of the complex is the same as that reported in the human reconstituted thin filament. A reconstruction of zebrafish cardiac F-actin demonstrates no deviations from human cardiac actin over an extended length of 14 actin subunits. Modelling zebrafish homology models into our maps enabled us to compare, in detail, the similarity with human models. The structural similarities of troponin-T in particular, a region known to contain a hypertrophic cardiomyopathy 'hotspot', confirm the suitability of zebrafish to study these disease-causing mutations.

PubMed: 37480427
DOI: 10.1007/s10974-023-09653-5

実験手法

ELECTRON MICROSCOPY (3.9 Å)