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. Author manuscript; available in PMC: 2009 Nov 9.
Published in final edited form as: Microbiology (Reading). 2007 Oct;153(Pt 10):3548–3562. doi: 10.1099/mic.0.2007/007930-0

Fig. 5.

Fig. 5

(a) Sequence alignment of CysGB from the two heliobacterial species with the CysGB domain of the CysG protein of S. enterica for which a crystal structure is available (1PJS). (b) 3D model of CysGB for Hb. mobilis based on the above alignment. The bifunctional enzyme has two distinct structural domains, the dehydrogenase domain on the N terminus and the ferrochelatase domain on the C terminus. The bound cofactor NAD for the dehydrogenase domain is also shown.