8HBH

Structure of human soluble guanylate cyclase in the NO-activated state at 3.1 angstrom

Summary for 8HBH

• Entry DOI: 10.2210/pdb8hbh/pdb
• EMDB information: 34628 34632 34633 34634 34635
• Descriptor: Guanylate cyclase soluble subunit alpha-1, Guanylate cyclase soluble subunit beta-1, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: soluble guanylate cyclase, signaling protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 149382.11

Authors

Chen, L.,Liu, R. (deposition date: 2022-10-28, release date: 2023-04-19, Last modification date: 2024-07-03)

Primary citation

Liu, R.,Kang, Y.,Chen, L.
NO binds to the distal site of haem in the fully activated soluble guanylate cyclase.
Nitric Oxide, 134-135:17-22, 2023

PubMed Abstract: Soluble guanylate cyclase (sGC) is the primary receptor for nitric oxide (NO). The binding of NO to the haem of sGC induces a large conformational change in the enzyme and activates its cyclase activity. However, whether NO binds to the proximal site or the distal site of haem in the fully activated state remains under debate. Here, we present cryo-EM maps of sGC in the NO-activated state at high resolutions, allowing the observation of the density of NO. These cryo-EM maps show the binding of NO to the distal site of haem in the NO-activated state.

PubMed: 36972843
DOI: 10.1016/j.niox.2023.03.002

Experimental method

ELECTRON MICROSCOPY (3.1 Å)