6KGE

Crystal structure of CaDoc0917(R16D)-CaCohA2 complex at pH 5.5

6KGE の概要

• エントリーDOI: 10.2210/pdb6kge/pdb
• 関連するPDBエントリー: 6KG8 6KG9 6KGC 6KGD 6KGF
• 分子名称: Probably cellulosomal scaffolding protein, secreted cellulose-binding and cohesin domain, And cellulose-binding endoglucanase family 9 CelL ortholog dockerin domain, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: cohesin, dockerin, cellulosome, calcium-binding, hydrolase
• 由来する生物種: Clostridium acetobutylicum ATCC 824; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 44577.85

構造登録者

Feng, Y.,Yao, X. (登録日: 2019-07-11, 公開日: 2020-07-08, 最終更新日: 2023-11-22)

主引用文献

Yao, X.,Chen, C.,Wang, Y.,Dong, S.,Liu, Y.J.,Li, Y.,Cui, Z.,Gong, W.,Perrett, S.,Yao, L.,Lamed, R.,Bayer, E.A.,Cui, Q.,Feng, Y.
Discovery and mechanism of a pH-dependent dual-binding-site switch in the interaction of a pair of protein modules.
Sci Adv, 6:-, 2020

PubMed Abstract: Many important proteins undergo pH-dependent conformational changes resulting in "on-off" switches for protein function, which are essential for regulation of life processes and have wide application potential. Here, we report a pair of cellulosomal assembly modules, comprising a cohesin and a dockerin from , which interact together following a unique pH-dependent switch between two functional sites rather than on-off states. The two cohesin-binding sites on the dockerin are switched from one to the other at pH 4.8 and 7.5 with a 180° rotation of the bound dockerin. Combined analysis by nuclear magnetic resonance spectroscopy, crystal structure determination, mutagenesis, and isothermal titration calorimetry elucidates the chemical and structural mechanism of the pH-dependent switching of the binding sites. The pH-dependent dual-binding-site switch not only represents an elegant example of biological regulation but also provides a new approach for developing pH-dependent protein devices and biomaterials beyond an on-off switch for biotechnological applications.

PubMed: 33097546
DOI: 10.1126/sciadv.abd7182

実験手法

X-RAY DIFFRACTION (2 Å)