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. Author manuscript; available in PMC: 2015 Apr 8.
Published in final edited form as: Structure. 2014 Feb 20;22(4):602–611. doi: 10.1016/j.str.2014.01.008

Figure 1. Domain organization of sGC subunits and truncations.

Figure 1

The sGC holoenzyme consists of two homologous subunits, α1 (gray) and β1 (tan), each composed of four domains. NO binds to the ferrous heme cofactor (red) of the β1 H-NOX domain. Cyclization of GTP (green) to cGMP occurs in the C-terminal catalytic domains. Truncations of the β1 sGC subunit preserve NO-binding. β1[1-194] comprises the minimal heme-binding H-NOX domain. β1[1-385] includes the associated PAS domain and a portion of the helical domain.