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. 2008 Sep 23;36(18):5992–6003. doi: 10.1093/nar/gkn588

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© 2008 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 7. — Active-site determination. (A) Weblogo showing the conservation of residues at the putative active site core in the C-terminal region of XseA. Residues D235 and D240 are the two conserved aspartic acid residues (highlighted by black stars) that were mutated to alanines. (B) Activity assay comparing purified WT and D235A/D240A mutant (labeled AA) T. maritima ExoVII. Although the two proteins were purified using the same procedure and exhibited identical solution properties, the D235A/D240A mutant is completely inactive.