7MWQ

Structure of De Novo designed beta sheet heterodimer LHD29A53/B53

Summary for 7MWQ

• Entry DOI: 10.2210/pdb7mwq/pdb
• Descriptor: LHD29A53, LHD29B53 (3 entities in total)
• Functional Keywords: de novo design, beta-sheet, heterodimer, de novo protein
• Biological source: synthetic construct; More
• Total number of polymer chains: 4
• Total formula weight: 92352.51

Authors

Bera, A.K.,Sahtoe, D.D.,Kang, A.,Praetorius, F.,Baker, D. (deposition date: 2021-05-17, release date: 2022-01-19, Last modification date: 2024-04-03)

Primary citation

Sahtoe, D.D.,Praetorius, F.,Courbet, A.,Hsia, Y.,Wicky, B.I.M.,Edman, N.I.,Miller, L.M.,Timmermans, B.J.R.,Decarreau, J.,Morris, H.M.,Kang, A.,Bera, A.K.,Baker, D.
Reconfigurable asymmetric protein assemblies through implicit negative design.
Science, 375:eabj7662-eabj7662, 2022

PubMed Abstract: Asymmetric multiprotein complexes that undergo subunit exchange play central roles in biology but present a challenge for design because the components must not only contain interfaces that enable reversible association but also be stable and well behaved in isolation. We use implicit negative design to generate β sheet-mediated heterodimers that can be assembled into a wide variety of complexes. The designs are stable, folded, and soluble in isolation and rapidly assemble upon mixing, and crystal structures are close to the computational models. We construct linearly arranged hetero-oligomers with up to six different components, branched hetero-oligomers, closed C4-symmetric two-component rings, and hetero-oligomers assembled on a cyclic homo-oligomeric central hub and demonstrate that such complexes can readily reconfigure through subunit exchange. Our approach provides a general route to designing asymmetric reconfigurable protein systems.

PubMed: 35050655
DOI: 10.1126/science.abj7662

Experimental method

X-RAY DIFFRACTION (2.56 Å)