Structural analyses unravel the molecular mechanism of cyclic di-GMP regulation of bacterial chemotaxis via a PilZ adaptor protein

• Main Authors: Yan, Xin-Fu, Xin, Lingyi, Yen, Jackie Tan, Zeng, Yukai, Jin, Shengyang, Cheang, Qing Wei, Fong, Rachel Andrea Chea Yuen, Chiam, Keng-Hwee, Liang, Zhao-Xun, Gao, Yong-Gui
• Other Authors: School of Biological Sciences
• Format: Article
• Language: English
• Published: 2018
• Subjects: Chemotaxis; Crystal Structure
• Online Access: https://hdl.handle.net/10356/87353; http://hdl.handle.net/10220/44396
• Institution: Nanyang Technological University

The bacterial second messenger cyclic di-GMP (c-di-GMP) has emerged as a prominent mediator of bacterial physiology, motility, and pathogenicity. c-di-GMP often regulates the function of its protein targets through a unique mechanism that involves a discrete PilZ adaptor protein. However, the molecu...