Figure_6.tif (949.33 kB)
Proposed model of the heterodimeric sGC enzyme complex based on the results of FRET analysis and fusion of sGC subunits.
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posted on 2010-07-15, 00:23 authored by Tobias Haase, Nadine Haase, Jan Robert Kraehling, Soenke BehrendsThe dimensions of the domains are given on the basis of the crystal structures of domain homologues (H-NOX, PDB ID 2O09 [9]; PAS, PDB ID 2P04 [13]; cat PDB ID 3ET6 [5]) and the structure of the coiled coil domain of the β1 subunit (PDB ID 3HLS [18]). Elongated model of the sGC (A). Model according to our results (B). Model of fluorescent-conjoined sGC (C). The β1 subunit is shown in red and the α subunit is shown in blue. cat - catalytic domain, CC - coiled coil region, PAS - Per-Arnt-Sim fold, HNOX - heme nitric oxide/oxygen binding domain.