PDBsum entry 6e5c

De novo protein

PDB id: 6e5c

Contents

Protein chain

78 a.a.

PDB id:

6e5c

Name:

De novo protein

Title:

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

Structure:

De novo beta protein. Chain: a. Engineered: yes

Source:

Synthetic construct. Organism_taxid: 32630. Expressed in: escherichia coli. Expression_system_taxid: 562

NMR struc:

10 models

Authors:

E.Marcos,T.M.Chidyausiku,A.Mcshan,T.Evangelidis,S.Nerli,N.Sgourakis, K.Tripsianes,D.Baker

Key ref:

E.Marcos et al. (2018). De novo design of a non-local β-sheet protein with high stability and accuracy. Nat Struct Mol Biol, 25, 1028-1034. PubMed id: 30374087

Date:

19-Jul-18 Release date: 07-Nov-18

Protein chain

No UniProt id for this chain

Struc: 78 a.a.

Nat Struct Mol Biol 25:1028-1034 (2018)

PubMed id: 30374087

De novo design of a non-local β-sheet protein with high stability and accuracy.

E.Marcos, T.M.Chidyausiku, A.C.McShan, T.Evangelidis, S.Nerli, L.Carter, L.G.Nivón, A.Davis, G.Oberdorfer, K.Tripsianes, N.G.Sgourakis, D.Baker.

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.