The Lrp Family of Transcription Regulators in Archaea
Figure 1
Structural features of archaeal Lrp-like proteins. (a) Monomeric structure of Grp from S. tokodaii (PDB 2E7W) [31]. Secondary structure elements are named as follows: α-helices are called αA–αE and β-strands β1–β5. The N-terminal DNA-binding domain corresponds to the bottom part of the structure, the C-terminal ligand binding domain to the top part. These are labeled DNA-binding domain and RAM domain, respectively. (b) Cocrystal structure of an FL11 dimer bound to DNA (PDB 2E1C) [30]. (c) Octameric structure of LrpA from P. furiosus (PDB 1I1G) [28]. (d) Cocrystal structure of an arginine-bound octamer of FL11 from P. horikoshii, which has an open conformation (PDB 2ZNY) [32]. The position of the arginine molecules is shown by purple symbols.
