Figure 1
From: Structural studies of the periplasmic portion of the diguanylate cyclase CdgH from Vibrio cholerae
The overall structure of the periplasmic portion of CdgH. (a) The domain architecture of the full-length Vibrio cholerae CdgH protein. (b) The overall structure of the periplasmic portion of CdgH (46–491aa). (c) The electron density found in the ligand-binding pocket was contoured at 3.0 σ in the |Fo| − |Fc| maps. The L-arginine fits well in the electron density omit map. (d) Data of the ITC experiment involving the refolded periplasmic portion of CdgH with L-arginine. (e,f) The similar folding topologies of the PBPb-I and -II domains. Lobe-I and lobe-II of the PBPb-I domain are shown in green and yellow, while lobe-I′ and lobe-II′ of the PBPb-II domain are shown in cyan and orange. The L-arginine bound in the ligand-binding pocket is shown in magenta.
