6IWJ

A designed domain swapped dimer

6IWJ の概要

• エントリーDOI: 10.2210/pdb6iwj/pdb
• 分子名称: Archeal Protein MK0293 (1 entity in total)
• 機能のキーワード: complex, domain-swapping, archea, protein design, unknown function
• 由来する生物種: Methanopyrus kandleri AV19
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22647.53

構造登録者

Nandwani, N.,Negi, H.,Das, R. (登録日: 2018-12-05, 公開日: 2019-02-13, 最終更新日: 2024-05-15)

主引用文献

Nandwani, N.,Surana, P.,Negi, H.,Mascarenhas, N.M.,Udgaonkar, J.B.,Das, R.,Gosavi, S.
A five-residue motif for the design of domain swapping in proteins.
Nat Commun, 10:452-452, 2019

PubMed Abstract: Domain swapping is the process by which identical monomeric proteins exchange structural elements to generate dimers/oligomers. Although engineered domain swapping is a compelling strategy for protein assembly, its application has been limited due to the lack of simple and reliable design approaches. Here, we demonstrate that the hydrophobic five-residue 'cystatin motif' (QVVAG) from the domain-swapping protein Stefin B, when engineered into a solvent-exposed, tight surface loop between two β-strands prevents the loop from folding back upon itself, and drives domain swapping in non-domain-swapping proteins. High-resolution structural studies demonstrate that engineering the QVVAG stretch independently into various surface loops of four structurally distinct non-domain-swapping proteins enabled the design of different modes of domain swapping in these proteins, including single, double and open-ended domain swapping. These results suggest that the introduction of the QVVAG motif can be used as a mutational approach for engineering domain swapping in diverse β-hairpin proteins.

PubMed: 30692525
DOI: 10.1038/s41467-019-08295-x

実験手法

SOLUTION NMR