Protein Family Models

Date:

2024-08-14

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)

Date:

2024-10-16

Rsp (repressor of surface proteins), as described in Staphylococcus aureus, is a large protein with an AraC-like helix-turn-helix DNA-binding domain. Regulatory targets include the accessory gene regulator (agr) operon, which in turn regulates a large number of virulence factors.

Gene:

rsp

Date:

2021-06-17