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. 2012 Jun 8;13(6):7109–7137. doi: 10.3390/ijms13067109

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© 2012 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.

This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).

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Structural comparison between apo-HpCopP and apo-CopZ. (A) The composition of cop ORFs of H. pylori and E. hirae; (B) The orientation of the two cysteines and one histidine in the CXXC motif of HpCopP is compared with that of EhCopZ. The hydrophobic protection by Tyr 64 in loop V stabilizes the Cu(I)-coordination in EhCopZ. This residue is highly conserved in bacterial proteins, but is replaced with Gln 63 in HpCopP. The side-chain of Gln 63 is not fully exposed to the solvent and points toward the metal binding site in apo-HpCopP. The structures of EhCopZ (PDB ID: 1CPZ) were obtained from the PDB; (C) The electrostatic potential surfaces of HpCopP and EhCopZ are compared to each other. The positively and negatively charged residues are represented in blue and red, respectively.