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. 2017 Jul 4;8:15952. doi: 10.1038/ncomms15952

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Copyright © 2017, The Author(s)

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(a) The nucleophilic elbow (orange) consisting of a β-strand-turn-helix (dashed box) shown in context of the overall Lnt structure (grey). (b) Expanded view of the boxed region in a showing the catalytic Cys387 in the turn. The oxyanion hole created by backbone amides in α3′ is indicated. (c) Coordination between residues in the turn and the α3′ helix. Dashed lines correspond to distances of ≤3.5 Å. (d) Residues in L1 are coordinated to the core of the MD via Arg139 in H5 and to the nucleophilic elbow via Tyr388.