Atomic structure of the regulatory TGS domain of Rel protein from Mycobacterium tuberculosis and its interaction with deacylated tRNA
The stringent response is critical for the survival of Mycobacterium tuberculosis (Mtb) under nutrient starvation. The mechanism is mediated by a GTP pyrophosphokinase known as Rel, containing N-terminal synthetase and hydrolase domains and C-terminal regulatory domains, which include the TGS domain...
Saved in:
Main Authors: | Shin, Joon, Singal, Bharti, Grüber, Ardina, Wong, David Meng Kit, Ragunathan, Priya, Grüber, Gerhard |
---|---|
Other Authors: | School of Biological Sciences |
Format: | Article |
Language: | English |
Published: |
2022
|
Subjects: | |
Online Access: | https://hdl.handle.net/10356/161762 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Institution: | Nanyang Technological University |
Language: | English |
Similar Items
-
Atomic structure of, and valine binding to the regulatory ACT domain of the Mycobacterium tuberculosis Rel protein
by: Shin, Joon, et al.
Published: (2021) -
Introduction : novel insights into TB research and drug discovery
by: Grüber, Gerhard
Published: (2020) -
Study of antimicrobial susceptibilities of mycobacterium tuberculosis by using resistance ratio method and proportion method
by: Sirimart Subpaiboon
Published: (2023) -
The unique C-terminal extension of mycobacterial F-ATP synthase subunit α is the major contributor to its latent ATP hydrolysis activity
by: Wong, Chui-Fann, et al.
Published: (2021) -
EthA/R-Independent Killing of Mycobacterium tuberculosis by Ethionamide
by: Ang, Michelle L. T., et al.
Published: (2017)