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

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

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...

Full description

Saved in:
Bibliographic Details
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
Tags: Add Tag
No Tags, Be the first to tag this record!
Institution: Nanyang Technological University
Language: English

Internet

https://hdl.handle.net/10356/87353
http://hdl.handle.net/10220/44396

Similar Items