Discovery and Mechanism of a PH-dependent Dual-binding-site Switch in the Interaction of a Pair of Protein Modules

Overview

Journal Sci Adv

Specialties Biology
Science

Date 2020 Oct 24

PMID 33097546

Citations 9

Authors

Xingzhe Yao

Chao Chen

Yefei Wang

Sheng Dong

Ya-Jun Liu

Yifei Li

Zhenling Cui

Weibin Gong

Sarah Perrett

Lishan Yao

Raphael Lamed

Edward A Bayer

Qiu Cui

Yingang Feng

Affiliations

Soon will be listed here.

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.

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