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. 2010 Dec 29;286(9):7301–7307. doi: 10.1074/jbc.M110.203315

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© 2011 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 2. — Stereo view of the direct and water-mediated hydrogen-bonding interactions between the prosequence of MTGase zymogen and the residues in the active-site cleft. Note the hydrogen bonds that are also formed between the main chain oxygen of Ala-10 and the main chain NH of Ser-349 and between the main chain NH of Tyr-12 and the Oδ1 of Asp-350, respectively. The side chains of Arg-72 and Tyr-70 are shifted compared with the structure of the mature MTGase because of the shift in the position of His-320 to form a hydrogen bond with the Oγ atom of Ser-339. This has not been shown, as it was not possible to generate a clear view.