8G8I

C3HR3_9r_shift4: Extendable repeat protein fiber

Summary for 8G8I

• Entry DOI: 10.2210/pdb8g8i/pdb
• EMDB information: 29680 29847 29849 29851 29856
• Descriptor: C3HR3_9r_shift4 (1 entity in total)
• Functional Keywords: oligomer, repeat protein, de novo protein
• Biological source: synthetic construct
• Total number of polymer chains: 5
• Total formula weight: 279610.60

Authors

Bethel, N.P.,Borst, A.J. (deposition date: 2023-02-17, release date: 2023-08-30, Last modification date: 2025-05-21)

Primary citation

Bethel, N.P.,Borst, A.J.,Parmeggiani, F.,Bick, M.J.,Brunette, T.J.,Nguyen, H.,Kang, A.,Bera, A.K.,Carter, L.,Miranda, M.C.,Kibler, R.D.,Lamb, M.,Li, X.,Sankaran, B.,Baker, D.
Precisely patterned nanofibres made from extendable protein multiplexes.
Nat.Chem., 15:1664-1671, 2023

PubMed Abstract: Molecular systems with coincident cyclic and superhelical symmetry axes have considerable advantages for materials design as they can be readily lengthened or shortened by changing the length of the constituent monomers. Among proteins, alpha-helical coiled coils have such symmetric, extendable architectures, but are limited by the relatively fixed geometry and flexibility of the helical protomers. Here we describe a systematic approach to generating modular and rigid repeat protein oligomers with coincident C to C and superhelical symmetry axes that can be readily extended by repeat propagation. From these building blocks, we demonstrate that a wide range of unbounded fibres can be systematically designed by introducing hydrophilic surface patches that force staggering of the monomers; the geometry of such fibres can be precisely tuned by varying the number of repeat units in the monomer and the placement of the hydrophilic patches.

PubMed: 37667012
DOI: 10.1038/s41557-023-01314-x

Experimental method

ELECTRON MICROSCOPY (3.92 Å)