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. 2010 Sep 15;39(2):623–634. doi: 10.1093/nar/gkq802

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© The Author(s) 2010. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), 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. — Catalytic mechanism of wild-type EndA: the proposed catalytic mechanism of EndA is based on the established catalytic mechanism of the Serratia nuclease (26). His160 acts as the general base for the activation of a water molecule. The magnesium ion is coordinated by Asn191, which is held in place by Asp157, and the proS-oxygen as well as the 3′-oxygen of the phosphate diester. A glutamic acid residue residue nearby (Glu196 or Glu205 in EndA) is assumed to be indirectly involved in water-mediated magnesium ion binding.