PDBsum entry 4m6a

De novo protein

PDB id: 4m6a

Contents

Protein chains

87 a.a.

(+ 2 more) 91 a.a.

Waters ×182

PDB id:

4m6a

Name:

De novo protein

Title:

N-terminal beta-strand swapping in a consensus derived alternative scaffold driven by stabilizing hydrophobic interactions

Structure:

Tencon. Chain: a, b, c, d, e, f, g, h, i, j. Fragment: fn3-like domain. Engineered: yes

Source:

Synthetic construct. Organism_taxid: 32630. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.71Å R-factor: 0.235 R-free: 0.290

Authors:

J.Luo,A.Teplyakov,G.Obmolova,T.J.Malia,W.Chan,S.A.Jocobs,K.T.O'Neil, G.L.Gilliland

Key ref:

J.Luo et al. (2014). N-terminal β-strand swapping in a consensus-derived alternative scaffold driven by stabilizing hydrophobic interactions. Proteins, 82, 1527-1533. PubMed id: 24464739 DOI: 10.1002/prot.24517

Date:

09-Aug-13 Release date: 26-Feb-14

Protein chains

No UniProt id for this chain

Struc: 87 a.a.

Protein chains

No UniProt id for this chain

Struc: 91 a.a.

DOI no: 10.1002/prot.24517

Proteins 82:1527-1533 (2014)

PubMed id: 24464739

N-terminal β-strand swapping in a consensus-derived alternative scaffold driven by stabilizing hydrophobic interactions.

J.Luo, A.Teplyakov, G.Obmolova, T.J.Malia, W.Chan, S.A.Jacobs, K.T.O'Neil, G.L.Gilliland.

ABSTRACT

The crystal structure of an N-terminal β-strand-swapped consensus-derived tenascin FN3 alternative scaffold has been determined. A comparison with the unswapped structure reveals that the side chain of residue F88 orients differently and packs more tightly with the hydrophobic core of the domain. Dimer formation also results in the burial of a hydrophobic patch on the surface of the domain. Thus, it appears that tighter packing of F88 in the hydrophobic core and burial of surface hydrophobicity provide the driving forces for the N-terminal β-strand swapping, leading to the formation of a stable compact dimer. Proteins 2014; 82:1527-1533. © 2014 Wiley Periodicals, Inc.