Structural insights into the mechanism of human soluble guanylate cyclase

Yunlu Kang, Rui Liu, Jing-Xiang Wu and Lei Chen ()
Additional contact information
Yunlu Kang: Peking University, Beijing Key Laboratory of Cardiometabolic Molecular Medicine
Rui Liu: Peking University, Beijing Key Laboratory of Cardiometabolic Molecular Medicine
Jing-Xiang Wu: Peking University, Beijing Key Laboratory of Cardiometabolic Molecular Medicine
Lei Chen: Peking University, Beijing Key Laboratory of Cardiometabolic Molecular Medicine

Nature, 2019, vol. 574, issue 7777, 206-210

Abstract: Abstract Soluble guanylate cyclase (sGC) is the primary sensor of nitric oxide. It has a central role in nitric oxide signalling and has been implicated in many essential physiological processes and disease conditions. The binding of nitric oxide boosts the enzymatic activity of sGC. However, the mechanism by which nitric oxide activates the enzyme is unclear. Here we report the cryo-electron microscopy structures of the human sGCα1β1 heterodimer in different functional states. These structures revealed that the transducer module bridges the nitric oxide sensor module and the catalytic module. Binding of nitric oxide to the β1 haem-nitric oxide and oxygen binding (H-NOX) domain triggers the structural rearrangement of the sensor module and a conformational switch of the transducer module from bending to straightening. The resulting movement of the N termini of the catalytic domains drives structural changes within the catalytic module, which in turn boost the enzymatic activity of sGC.

Date: 2019
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/s41586-019-1584-6 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:574:y:2019:i:7777:d:10.1038_s41586-019-1584-6

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/s41586-019-1584-6

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().