3N3E

Zebrafish AlphaA crystallin

3N3E の概要

• エントリーDOI: 10.2210/pdb3n3e/pdb
• 分子名称: Alpha A crystallin (2 entities in total)
• 機能のキーワード: protein chaperone, eye lens transparency, chaperone
• 由来する生物種: Danio rerio (leopard danio,zebra danio,zebra fish)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 23918.44

構造登録者

Laganowsky, A.,Eisenberg, D. (登録日: 2010-05-19, 公開日: 2010-08-11, 最終更新日: 2023-09-06)

主引用文献

Laganowsky, A.,Eisenberg, D.
Non-3D domain swapped crystal structure of truncated zebrafish alphaA crystallin.
Protein Sci., 19:1978-1984, 2010

PubMed Abstract: In previous work on truncated alpha crystallins (Laganowsky et al., Protein Sci 2010; 19:1031-1043), we determined crystal structures of the alpha crystallin core, a seven beta-stranded immunoglobulin-like domain, with its conserved C-terminal extension. These extensions swap into neighboring cores forming oligomeric assemblies. The extension is palindromic in sequence, binding in either of two directions. Here, we report the crystal structure of a truncated alphaA crystallin (AAC) from zebrafish (Danio rerio) revealing C-terminal extensions in a non three-dimensional (3D) domain swapped, "closed" state. The extension is quasi-palindromic, bound within its own zebrafish core domain, lying in the opposite direction to that of bovine AAC, which is bound within an adjacent core domain (Laganowsky et al., Protein Sci 2010; 19:1031-1043). Our findings establish that the C-terminal extension of alpha crystallin proteins can be either 3D domain swapped or non-3D domain swapped. This duality provides another molecular mechanism for alpha crystallin proteins to maintain the polydispersity that is crucial for eye lens transparency.

PubMed: 20669149
DOI: 10.1002/pro.471

実験手法

X-RAY DIFFRACTION (1.75 Å)