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helix-turn-helix domain-containing protein
PocR ligand-binding domain-containing protein
PocR, a ligand binding domain, has a novel variant of the PAS-like Fold. Evidence suggests that it binds small hydrocarbon derivatives such as 1,3-propanediol [1]. In (Natural history of sensor domains in bacterial signaling systems by Aravind L, LM Iyer, Anantharaman V, from 'Sensory Mechanisms in Bacteria: Molecular Aspects of Signal Recognition.' Caister Academic Press. 2010) - see (http://de.scribd.com/doc/28576661/Bacterial-Signaling-Chapter) [1]. 15814558. MEDS and PocR are novel domains with a predicted role in sensing. simple hydrocarbon derivatives in prokaryotic signal. transduction systems.. Anantharaman V, Aravind L;. Bioinformatics. 2005;21:2805-2811. (from Pfam)
AraC family transcriptional regulator
In the absence of arabinose, the N-terminal arm of AraC binds to the DNA binding domain (Pfam:PF00165) and helps to hold the two DNA binding domains in a relative orientation that favours DNA looping. In the presence of arabinose, the arms bind over the arabinose on the dimerisation domain, thus freeing the DNA-binding domains. The freed DNA-binding domains are then able to assume a conformation suitable for binding to the adjacent DNA sites that are utilised when AraC activates transcription, and hence AraC ceases looping the DNA when arabinose is added [1-2]. [1]. 9600836. Apo-AraC actively seeks to loop.. Seabold RR, Schleif RF;. J Mol Biol 1998;278:529-538.. [2]. 9600837. Arm-domain interactions in AraC.. Saviola B, Seabold R, Schleif RF;. J Mol Biol 1998;278:539-548. (from Pfam)
PocR and AraC domain-containing protein
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