6IDC

Loop deletion and proline insertion mutant (deleting six residues and inserted six proline residues)

6IDC の概要

• エントリーDOI: 10.2210/pdb6idc/pdb
• 分子名称: Outer surface protein A (2 entities in total)
• 機能のキーワード: outer surface protein a, lipid binding protein, de novo protein
• 由来する生物種: Borrelia burgdorferi
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26445.66

構造登録者

Shiga, S.,Makabe, K. (登録日: 2018-09-09, 公開日: 2019-07-03, 最終更新日: 2023-11-22)

主引用文献

Shiga, S.,Yamanaka, M.,Fujiwara, W.,Hirota, S.,Goda, S.,Makabe, K.
Domain-Swapping Design by Polyproline Rod Insertion.
Chembiochem, 20:2454-2457, 2019

PubMed Abstract: During domain swapping, proteins mutually interconvert structural elements to form a di-/oligomer. Engineering this process by design is important for creating a higher order protein assembly with minimal modification. Herein, a simple design strategy is shown for domain-swapping formation by loop deletion and insertion of a polyproline rod. Crystal structures revealed the formation of the domain-swapped dimers and polyproline portion formed a polyproline II (PPII) structure. Small-angle X-ray scattering demonstrated that an extended orientation of domain-swapped dimer was retained in solution. It is found that a multiple of three of inserting proline residue is favored for domain swapping because of the helical nature of PPII. The rigid nature of the polyproline rod enables precise control of the interdomain distance and orientation.

PubMed: 31094059
DOI: 10.1002/cbic.201900179

実験手法

X-RAY DIFFRACTION (2.007 Å)