Figure 3 - full size

 

Figure 3.
Figure 3. Structural comparison between the URN1FF domain and other related structures. (A) Structure-based alignment of FF and SURP aligned profiles. Conserved residues between the two profiles are indicated with red gradient (FFs) and blue gradient (SURPs) backgrounds according to the degree of conservation (dark is the most conserved). For instance, in the FF family the Phe in the first helix (the one corresponding to the first Phe in the name FF) is conserved in all sequences, while the SURP family contains an Ala at this equivalent position. Both families have a pair of hydrophobic semiconserved residues in position +3 with respect to this Phe/Ala highly conserved residue. Similarly, in the last helix there are four positions conserved in each family, but not between the families. Secondary structure elements for each profile and residue numbers of the distinct domains are indicated. (B) Left and right: URN1FF domain (in orange) superimposed to either DEK C-term structure (in green, PDB code 1Q1V) or the SF3a120SURP1 structure (in blue, PDB code 2DT6). Representations show the superimpositions according to the 1- 3 fittings using the optAlign alignment script. Secondary structure elements are indicated. (C) RMSD of the family representatives for another 3-helical bundle fold, as well as for the SF3a120SURP1 domain (in bold) with respect to the URN1FF. Fittings were generated taking either the secondary structure elements 1- 3 helices or the whole molecules (Global). PDB codes: C-term S/T phosphatase 2C-1A6Q, B-form DNA-mimic Ocr-1S7Z, DEK-C-term-1Q1V, IscX protein-1UJ8, SF3a120SURP1-2DT6.

The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2008, 73, 1001-1009) copyright 2008.