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. Author manuscript; available in PMC: 2014 Dec 10.
Published in final edited form as: Biochemistry. 2013 Nov 25;52(49):8916–8928. doi: 10.1021/bi400988t

Figure 7.

Figure 7

The 1.82 Å-resolution structure of RifDH10. a) The 2Fo-Fc electron density map (contoured at 1.8 σ) shows a water molecule, bound to the catalytic histidine (H50) and aspartate (D220), as well as a nearly invariant Y174, that is representative of the water molecule eliminated through a syn-dehydration reaction. H224 and Y164 may help increase the pKa of D220 through a hydrogen-bond network. b) Stereodiagram of the superposition of the active sites of RifDH10, EryDH4, CurF DH, CurH DH, CurJ DH, and CurK DH, showing the catalytic His (H) and Asp (D) residues.