5COC

Fusion protein of human calmodulin and B4 domain of protein A from staphylococcal aureus

5COC の概要

• エントリーDOI: 10.2210/pdb5coc/pdb
• 分子名称: Immunoglobulin G-binding protein A,Calmodulin, CALCIUM ION (3 entities in total)
• 機能のキーワード: fusion, alpha helix, cross-linker, protein binding
• 由来する生物種: Staphylococcus aureus; 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton, spindle : P62158
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14630.27

構造登録者

Jeong, W.H.,Lee, H.,Song, D.H.,Lee, J.O. (登録日: 2015-07-20, 公開日: 2016-03-30, 最終更新日: 2024-11-06)

主引用文献

Jeong, W.H.,Lee, H.,Song, D.H.,Eom, J.H.,Kim, S.C.,Lee, H.S.,Lee, H.,Lee, J.O.
Connecting two proteins using a fusion alpha helix stabilized by a chemical cross linker.
Nat Commun, 7:11031-11031, 2016

PubMed Abstract: Building a sophisticated protein nano-assembly requires a method for linking protein components in a predictable and stable structure. Most of the cross linkers available have flexible spacers. Because of this, the linked hybrids have significant structural flexibility and the relative structure between their two components is largely unpredictable. Here we describe a method of connecting two proteins via a 'fusion α helix' formed by joining two pre-existing helices into a single extended helix. Because simple ligation of two helices does not guarantee the formation of a continuous helix, we used EY-CBS, a synthetic cross linker that has been shown to react selectively with cysteines in α-helices, to stabilize the connecting helix. Formation and stabilization of the fusion helix was confirmed by determining the crystal structures of the fusion proteins with and without bound EY-CBS. Our method should be widely applicable for linking protein building blocks to generate predictable structures.

PubMed: 26980593
DOI: 10.1038/ncomms11031

実験手法

X-RAY DIFFRACTION (2.6691 Å)