Language:

Structural insights into the signalling mechanisms of two-component systems

Nature reviews. Microbiology, 2018-10, Vol.16 (10), p.585-593 [Peer Reviewed Journal]

COPYRIGHT 2018 Nature Publishing Group ;Copyright Nature Publishing Group Oct 2018 ;Distributed under a Creative Commons Attribution 4.0 International License ;ISSN: 1740-1526 ;EISSN: 1740-1534 ;DOI: 10.1038/s41579-018-0055-7 ;PMID: 30008469

Full text available

Citations Cited by

Actions
1. Add to My Research
2. Remove from My Research
3. E-mail
4. Print
5. Permalink
6. Citation
7. EasyBib
8. EndNote
9. RefWorks
10. Delicious
11. Export RIS
12. Export BibTeX

Title:
Structural insights into the signalling mechanisms of two-component systems
Author: Jacob-Dubuisson, Françoise ; Mechaly, Ariel ; Betton, Jean-Michel ; Antoine, Rudy
Subjects: Bacteria - chemistry ; Bacteria - enzymology ; Bacteria - metabolism ; Bacterial Proteins - chemistry ; Bacterial Proteins - metabolism ; Bacterial Proteins - physiology ; Biochemistry, Molecular Biology ; Catalysis ; Cellular signal transduction ; Conformation ; Crystal structure ; Cytoplasm - chemistry ; Cytoplasm - metabolism ; Cytoplasm - physiology ; Dephosphorylation ; Domains ; Enzymes ; Genetic aspects ; Health aspects ; Histidine ; Histidine kinase ; Histidine Kinase - chemistry ; Histidine Kinase - metabolism ; Histidine Kinase - physiology ; Kinases ; Life Sciences ; Microorganisms ; Models, Molecular ; Molecular machines ; Phosphatases ; Phosphorylation - physiology ; Phosphotransferases ; Properties ; Protein structure ; Sensors ; Signal transduction ; Signal Transduction - physiology ; Signaling ; Structural Biology ; Testing
Is Part Of: Nature reviews. Microbiology, 2018-10, Vol.16 (10), p.585-593
Description: Two-component systems reprogramme diverse aspects of microbial physiology in response to environmental cues. Canonical systems are composed of a transmembrane sensor histidine kinase and its cognate response regulator. They catalyse three reactions: autophosphorylation of the histidine kinase, transfer of the phosphoryl group to the regulator and dephosphorylation of the phosphoregulator. Elucidating signal transduction between sensor and output domains is highly challenging given the size, flexibility and dynamics of histidine kinases. However, recent structural work has provided snapshots of the catalytic mechanisms of the three enzymatic reactions and described the conformation and dynamics of the enzymatic moiety in the kinase-competent and phosphatase-competent states. Insight into signalling mechanisms across the membrane is also starting to emerge from new crystal structures encompassing both sensor and transducer domains of sensor histidine kinases. In this Progress article, we highlight such important advances towards understanding at the molecular level the signal transduction mechanisms mediated by these fascinating molecular machines.
Publisher: England: Nature Publishing Group
Language: English
Identifier: ISSN: 1740-1526
EISSN: 1740-1534
DOI: 10.1038/s41579-018-0055-7
PMID: 30008469
Source: MEDLINE
ProQuest Central

Back to results list


INSPIRE LIBRARY - TON DUC THANG UNIVERSITY	(84-028) 37 755 057	Feedback
19 Nguyen Huu Tho St. Dist.7, HCM	thuvien@tdtu.edu.vn	Feedback

Structural insights into the signalling mechanisms of two-component systems

COPYRIGHT 2018 Nature Publishing Group ;Copyright Nature Publishing Group Oct 2018 ;Distributed under a Creative Commons Attribution 4.0 International License ;ISSN: 1740-1526 ;EISSN: 1740-1534 ;DOI: 10.1038/s41579-018-0055-7 ;PMID: 30008469

Searching Remote Databases, Please Wait