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Fig. 3 | Mobile DNA

Fig. 3

From: The unusual structure of the PiggyMac cysteine-rich domain reveals zinc finger diversity in PiggyBac-related transposases

Fig. 3

Structure of the Pgm CRD. a Backbone superposition on residues (701–751) of the best 15 structures generated with CYANA, with the two anti-parallel β-sheets in pink and blue, the two longest α-helices in orange (the secondary elements are highlighted according to the BMRB protein structure validation suite result report) and Zn2+ ions in purple. The same color code is used in all panels. b The cysteine and histidine residues involved in the coordination of Zn2+ ions are shown as sticks and colored by atom types: His701, Cys723, Cys726, His749 (blue) and Cys712, Cys715, Cys737, Cys745 (pink) are respectively involved in the formation of each of the two zinc-binding motifs. Atoms from His738, which is not implicated in Zn2+ coordination, are colored in green. c Topology diagram of Pgm(692–768). d Topology diagram of the C1 domain of Rho-associated protein kinase 2 (ROCK II) (PDB id 2ROW). e Structure of the ROCK II C1 domain. f Topology diagram of the typical PHD domain. In panels c, d and f, Zn2+ coordination is highlighted by dotted lines. Only Zn2+-coordinating histidine residues are indicated (H, in green), all others ligands are cysteine residues (not indicated). β-strands are represented as arrows, helices as cylinders and Zinc ions as purple spheres

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