Figure 1
From: Structural Insight of the Full-Length Ros Protein: A Prototype of the Prokaryotic Zinc-Finger Family
(a) Ros sequence. Full-length Ros protein primary sequence: in red is highlighted the C-terminal globular domain (amino acids 56–142, Ros87) and in blue the additional region of del29-Ros (amino acids 30–55). The secondary structure elements of the NMR structure (β1 -amino acids 72 and 73-, β2 -from 76 to 78-, β3–85 and 86-, α1 -from 89 to 97- and α2 -from 101 to 108-) and of one of the proposed models (a′ -amino acids 6–27- and a′′ -amino acids 34–48- of M3) are represented under their corresponding sequences. (b-e) 3D structures. Structural models of the full-length Ros (amino acids 1–142; a-c) and of the N-term domain (amino acids 1–55; d) are shown in cartoon: a) M1, b) M2 and c) M3. Helices of the N-domain are rendered in yellow (α′), purple (α′′) and orange (α′′′ in M2). See main text. In C-domain (blue) zinc-coordinating residues are indicated in sticks and Zn(II) is a white sphere.
