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Figure 1
Crystal structures of (a) B8FYU2_DESHY, (b) Q9HJ63_THEAC and (c) Q2LQ23_SYNAS. The polypeptide backbones are shown as stereo ribbon diagrams. Below the ribbon representations are the secondary-structure elements superimposed on the primary sequence. The α-helices, 310-helices, β-strands, β-turns and γ-turns are indicated. β-Hairpins are depicted as red loops. (a) For B8FYU2_DESHY, the protein ribbon is color-coded from the N-terminus (blue) to the C-terminus (red). Helices α1–α4 and β-­strands (β1–β6) are indicated. A dual-occupancy zinc/nickel-binding site in the vicinity of the putative active site on the α+β core and the zinc-finger domain is shown as a gray sphere. (b) For Q9HJ63_THEAC, helices α1–α10 and β-strands (β1–β11) are indicated. The subregions of the structure, the core domain (NTD), linker and C-terminal zinc-finger domain (CTD), and the background of the corresponding sequence are colored turquoise, orange and pink, respectively. Zn atoms are shown as gray spheres. (c) For Q2LQ23_SYNAS, helices H1–H10 and β-strands (β1–β7) are indicated with subregions of the structure colored as in (b). A chloride ion in the vicinity of the putative active site is shown as a magenta sphere and the Zn atom bound to the zinc-finger domain is shown as a gray sphere.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
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