6X1I

Two-Component D3 Assembly Constructed by Fusing Symmetric Oligomers to Coiled Coils

Summary for 6X1I

• Entry DOI: 10.2210/pdb6x1i/pdb
• Related: 1WY1 3DXO 4G1E
• Descriptor: Cob_adeno_trans domain-containing protein PH0671 fused to a coiled coil, SnoaL-like Protein fused to a coiled coil (2 entities in total)
• Functional Keywords: two-component, self-assembling, symmetric, d3, coiled coil, helical fusion, design, biosynthetic protein
• Biological source: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3); More
• Total number of polymer chains: 2
• Total formula weight: 37075.37

Authors

Laniado, J.,Yeates, T.O.,Sawaya, M.R. (deposition date: 2020-05-18, release date: 2021-03-03, Last modification date: 2023-10-18)

Primary citation

Laniado, J.,Cannon, K.A.,Miller, J.E.,Sawaya, M.R.,McNamara, D.E.,Yeates, T.O.
Geometric Lessons and Design Strategies for Nanoscale Protein Cages.
Acs Nano, 15:4277-4286, 2021

PubMed Abstract: Protein molecules bring a rich functionality to the field of designed nanoscale architectures. High-symmetry protein cages are rapidly finding diverse applications in biomedicine, nanotechnology, and imaging, but methods for their reliable and predictable construction remain challenging. In this study we introduce an approach for designing protein assemblies that combines ideas and favorable elements adapted from recent work. Cubically symmetric cages can be created by combining two simpler symmetries, following recently established principles. Here, two different oligomeric protein components are brought together in a geometrically specific arrangement by their separate genetic fusion to individual components of a heterodimeric coiled-coil polypeptide motif of known structure. Fusions between components are made by continuous α-helices to limit flexibility. After a computational design, we tested 10 different protein cage constructions experimentally, two of which formed larger assemblies. One produced the intended octahedral cage, ∼26 nm in diameter, while the other appeared to produce the intended tetrahedral cage as a minor component, crystallizing instead in an alternate form representing a collapsed structure of lower stoichiometry and symmetry. Geometric distinctions between the two characterized designs help explain the different degrees of success, leading to clearer principles and improved prospects for the routine creation of nanoscale protein architectures using diverse methods.

PubMed: 33683103
DOI: 10.1021/acsnano.0c07167

Experimental method

X-RAY DIFFRACTION (4.32 Å)