8GA6

Geometrically programmable nanomaterial construction using regularized protein building blocks

8GA6 の概要

• エントリーDOI: 10.2210/pdb8ga6/pdb
• 分子名称: THR6 (2 entities in total)
• 機能のキーワード: nanomaterial, protein building blocks, de novo design, train-track, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 54311.48

構造登録者

Huddy, T.,Bera, A.K.,Baker, D.,Kang, A. (登録日: 2023-02-22, 公開日: 2024-03-13, 最終更新日: 2024-04-10)

主引用文献

Huddy, T.F.,Hsia, Y.,Kibler, R.D.,Xu, J.,Bethel, N.,Nagarajan, D.,Redler, R.,Leung, P.J.Y.,Weidle, C.,Courbet, A.,Yang, E.C.,Bera, A.K.,Coudray, N.,Calise, S.J.,Davila-Hernandez, F.A.,Han, H.L.,Carr, K.D.,Li, Z.,McHugh, R.,Reggiano, G.,Kang, A.,Sankaran, B.,Dickinson, M.S.,Coventry, B.,Brunette, T.J.,Liu, Y.,Dauparas, J.,Borst, A.J.,Ekiert, D.,Kollman, J.M.,Bhabha, G.,Baker, D.
Blueprinting extendable nanomaterials with standardized protein blocks.
Nature, 627:898-904, 2024

PubMed Abstract: A wooden house frame consists of many different lumber pieces, but because of the regularity of these building blocks, the structure can be designed using straightforward geometrical principles. The design of multicomponent protein assemblies, in comparison, has been much more complex, largely owing to the irregular shapes of protein structures. Here we describe extendable linear, curved and angled protein building blocks, as well as inter-block interactions, that conform to specified geometric standards; assemblies designed using these blocks inherit their extendability and regular interaction surfaces, enabling them to be expanded or contracted by varying the number of modules, and reinforced with secondary struts. Using X-ray crystallography and electron microscopy, we validate nanomaterial designs ranging from simple polygonal and circular oligomers that can be concentrically nested, up to large polyhedral nanocages and unbounded straight 'train track' assemblies with reconfigurable sizes and geometries that can be readily blueprinted. Because of the complexity of protein structures and sequence-structure relationships, it has not previously been possible to build up large protein assemblies by deliberate placement of protein backbones onto a blank three-dimensional canvas; the simplicity and geometric regularity of our design platform now enables construction of protein nanomaterials according to 'back of an envelope' architectural blueprints.

PubMed: 38480887
DOI: 10.1038/s41586-024-07188-4

実験手法

X-RAY DIFFRACTION (2.5 Å)