6E5C

Solution NMR structure of a de novo designed double-stranded beta-helix

Summary for 6E5C

• Entry DOI: 10.2210/pdb6e5c/pdb
• NMR Information: BMRB: 30495
• Descriptor: De novo beta protein (1 entity in total)
• Functional Keywords: beta sheet, beta protein, de novo, de novo protein
• Biological source: synthetic construct
• Total number of polymer chains: 1
• Total formula weight: 8916.92

Authors

Marcos, E.,Chidyausiku, T.M.,McShan, A.,Evangelidis, T.,Nerli, S.,Sgourakis, N.,Tripsianes, K.,Baker, D. (deposition date: 2018-07-19, release date: 2018-11-07, Last modification date: 2024-05-01)

Primary citation

Marcos, E.,Chidyausiku, T.M.,McShan, A.C.,Evangelidis, T.,Nerli, S.,Carter, L.,Nivon, L.G.,Davis, A.,Oberdorfer, G.,Tripsianes, K.,Sgourakis, N.G.,Baker, D.
De novo design of a non-local beta-sheet protein with high stability and accuracy.
Nat. Struct. Mol. Biol., 25:1028-1034, 2018

PubMed Abstract: β-sheet proteins carry out critical functions in biology, and hence are attractive scaffolds for computational protein design. Despite this potential, de novo design of all-β-sheet proteins from first principles lags far behind the design of all-α or mixed-αβ domains owing to their non-local nature and the tendency of exposed β-strand edges to aggregate. Through study of loops connecting unpaired β-strands (β-arches), we have identified a series of structural relationships between loop geometry, side chain directionality and β-strand length that arise from hydrogen bonding and packing constraints on regular β-sheet structures. We use these rules to de novo design jellyroll structures with double-stranded β-helices formed by eight antiparallel β-strands. The nuclear magnetic resonance structure of a hyperthermostable design closely matched the computational model, demonstrating accurate control over the β-sheet structure and loop geometry. Our results open the door to the design of a broad range of non-local β-sheet protein structures.

PubMed: 30374087
DOI: 10.1038/s41594-018-0141-6

Experimental method

SOLUTION NMR