7DYA

Crystal structure of TmFtn with calcium ions

7DYA の概要

• エントリーDOI: 10.2210/pdb7dya/pdb
• 分子名称: Ferritin, FE (III) ION, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: thermotoga maritima ferritin, calcium ions, protein binding
• 由来する生物種: Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 156468.94

構造登録者

Zhang, X.,Zhao, G. (登録日: 2021-01-20, 公開日: 2021-09-01, 最終更新日: 2023-11-29)

主引用文献

Zhang, X.,Liu, Y.,Zheng, B.,Zang, J.,Lv, C.,Zhang, T.,Wang, H.,Zhao, G.
Protein interface redesign facilitates the transformation of nanocage building blocks to 1D and 2D nanomaterials.
Nat Commun, 12:4849-4849, 2021

PubMed Abstract: Although various artificial protein nanoarchitectures have been constructed, controlling the transformation between different protein assemblies has largely been unexplored. Here, we describe an approach to realize the self-assembly transformation of dimeric building blocks by adjusting their geometric arrangement. Thermotoga maritima ferritin (TmFtn) naturally occurs as a dimer; twelve of these dimers interact with each other in a head-to-side manner to generate 24-meric hollow protein nanocage in the presence of Ca or PEG. By tuning two contiguous dimeric proteins to interact in a fully or partially side-by-side fashion through protein interface redesign, we can render the self-assembly transformation of such dimeric building blocks from the protein nanocage to filament, nanorod and nanoribbon in response to multiple external stimuli. We show similar dimeric protein building blocks can generate three kinds of protein materials in a manner that highly resembles natural pentamer building blocks from viral capsids that form different protein assemblies.

PubMed: 34381032
DOI: 10.1038/s41467-021-25199-x

実験手法

X-RAY DIFFRACTION (2.197 Å)