Skip to main content
. Author manuscript; available in PMC: 2012 Aug 1.
Published in final edited form as: Nat Chem. 2011 Nov 27;4(2):118–123. doi: 10.1038/nchem.1201

Figure 1. Ribbon diagrams of the [Hg(II)]S[Zn(II)(H2O/OH )]N(CSL9PenL23H)3n+ parallel 3SCC (one of two different 3-helix bundles present in the asymmetric unit) at pH 8.5.

Figure 1

Shown are the main chain atoms represented as helical ribbons (cyan) and the Pen and His side chains in stick form (sulphur = yellow, nitrogen = blue, oxygen = red). a, One of two trimers found in the asymmetric unit of the crystal structure. b, a top down view of the structural trigonal thiolate site, Hg(II)S3, confirming the proposed structure of Hg(II) in Cys-containing TRI peptides.17 This metal site should mimic well the structural site in the metalloregulatory protein MerR.47 c, a side view of the tetrahedral catalytic site, Zn(II)N3O, which closely mimics carbonic anhydrase and matrix metalloproteinase active sites.1 All figures are shown with 2Fo-Fc electron density contoured at 1.5 σ overlaid.