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. 2013 Oct 7;13:19. doi: 10.1186/1472-6807-13-19

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Copyright © 2013 Urosev et al.; licensee BioMed Central Ltd.

This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Similarities between crystal contacts observed in c5321 and in HcpC and interactions of Hop with the C-terminus of its Hsp70 target (PDB ID 1ELW). A. Structural superposition highlights similar mode of interaction involving concave region of the super-helix (molecule 1) and the extended peptide conformation of the C-terminus (molecule 2). B. Close-up of the hydrogen bonding interactions between the conserved asparagine residue (molecule 1, N310 in c5321) and the main chain of the C-terminus peptide (molecule 2). Note that the additional asparagine residue in c5321 (N345) is also involved in interactions with the main chain.