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. 2009 Jul 22;37(20):6960–6969. doi: 10.1093/nar/gkp603

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© 2009 The Author(s)

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 3. — Comparison of RDs. (A) The RD1 (gold) and RD2 (magenta) of HsdR_Vv are superposed with HCV NS3 helicase (HCV, grey). The residues of the DECH sequence (DE××) for ATP hydrolysis are displayed with stick models. (B) Close-up view of ATP-binding site. The catalytic residues for ATP hydrolysis are displayed with stick models and Mg ion with a green dot and occupy positions structurally equivalent to HCV helicase. In other functionally related enzymes, the aromatic ring of a protein side chain (Phe) stacks with the base of adenine nucleotide.