5L0P

Symmetry-based assembly of a two-dimensional protein lattice

Summary for 5L0P

• Entry DOI: 10.2210/pdb5l0p/pdb
• Descriptor: Transcription factor ETV6, Transcription factor ETV6, Transcription factor ETV6, Ferric uptake regulation protein chimera (2 entities in total)
• Functional Keywords: design, lattice, 2d, assembly, de novo protein
• Biological source: Homo sapiens (Human); More
• Cellular location: Cytoplasm : P45599
• Total number of polymer chains: 1
• Total formula weight: 40559.73

Authors

Faham, S. (deposition date: 2016-07-27, release date: 2017-03-29, Last modification date: 2023-10-04)

Primary citation

Poulos, S.,Agah, S.,Jallah, N.,Faham, S.
Symmetry based assembly of a 2 dimensional protein lattice.
PLoS ONE, 12:e0174485-e0174485, 2017

PubMed Abstract: The design of proteins that self-assemble into higher order architectures is of great interest due to their potential application in nanotechnology. Specifically, the self-assembly of proteins into ordered lattices is of special interest to the field of structural biology. Here we designed a 2 dimensional (2D) protein lattice using a fusion of a tandem repeat of three TelSAM domains (TTT) to the Ferric uptake regulator (FUR) domain. We determined the structure of the designed (TTT-FUR) fusion protein to 2.3 Å by X-ray crystallographic methods. In agreement with the design, a 2D lattice composed of TelSAM fibers interdigitated by the FUR domain was observed. As expected, the fusion of a tandem repeat of three TelSAM domains formed 21 screw axis, and the self-assembly of the ordered oligomer was under pH control. We demonstrated that the fusion of TTT to a domain having a 2-fold symmetry, such as the FUR domain, can produce an ordered 2D lattice. The TTT-FUR system combines features from the rotational symmetry matching approach with the oligomer driven crystallization method. This TTT-FUR fusion was amenable to X-ray crystallographic methods, and is a promising crystallization chaperone.

PubMed: 28419162
DOI: 10.1371/journal.pone.0174485

Experimental method

X-RAY DIFFRACTION (2.3 Å)