7DY9

Thermotoga maritima ferritin mutant-FLAL

Summary for 7DY9

• Entry DOI: 10.2210/pdb7dy9/pdb
• Descriptor: Ferritin (2 entities in total)
• Functional Keywords: thermotoga maritima ferritin, mutant, recombination
• Biological source: Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
• Total number of polymer chains: 2
• Total formula weight: 38689.80

Authors

Zhao, G.,Zhang, X. (deposition date: 2021-01-20, release date: 2021-09-01, Last modification date: 2023-11-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.303 Å)