3AQT

CRYSTAL STRUCTURE OF RolR (NCGL1110) complex WITH ligand RESORCINOL

Summary for 3AQT

• Entry DOI: 10.2210/pdb3aqt/pdb
• Related: 3AQS
• Descriptor: Bacterial regulatory proteins, tetR family, RESORCINOL (3 entities in total)
• Functional Keywords: helix-turn-helix, all alpha, transcription, transcription regulation, transcription regulator, all helix, tetr family, transcriptional repressor, resorcinol binding, dna binding
• Biological source: Corynebacterium glutamicum (Brevibacterium flavum)
• Total number of polymer chains: 2
• Total formula weight: 54687.41

Authors

Li, D.F.,Zhang, N.,Hou, Y.J.,Liu, S.J.,Wang, D.C. (deposition date: 2010-11-18, release date: 2011-07-06, Last modification date: 2024-10-16)

Primary citation

Li, D.F.,Zhang, N.,Hou, Y.J.,Huang, Y.,Hu, Y.,Zhang, Y.,Liu, S.J.,Wang, D.C.
Crystal structures of the transcriptional repressor RolR reveals a novel recognition mechanism between inducer and regulator.
Plos One, 6:e19529-e19529, 2011

PubMed Abstract: Many members of the TetR family control the transcription of genes involved in multidrug resistance and pathogenicity. RolR (ResorcinolRegulator), the recently reported TetR-type regulator for aromatic catabolism from Corynebacterium glutamicum, distinguishes itself by low sequence similarities and different regulation from the previously known members of the TetR family. Here we report the crystal structures of RolR in its effector-bound (with resorcinol) and aop- forms at 2.5 Å and 3.6 Å, respectively. The structure of resorcinol-RolR complex reveal that the hydrogen-bonded network mediated by the four-residue motif (Asp94- Arg145- Arg148- Asp149) with two water molecules and the hydrophobic interaction via five residues (Phe107, Leu111, Leu114, Leu142, and Phe172) are the key factors for the recognition and binding between the resorcinol and RolR molecules. The center-to-center separation of the recognition helices h3-h3' is decreased upon effector-binding from 34.9 Å to 30.4 Å. This structural change results in that RolR was unsuitable for DNA binding. Those observations are distinct from that in other TetR members. Structure-based mutagenesis on RolR was carried out and the results confirmed the critical roles of the above mentioned residues for effector-binding specificity and affinity. Similar sequence searches and sequence alignments identified 29 RolR homologues from GenBank, and all the above mentioned residues are highly conserved in the homologues. Based on these structural and other functional investigations, it is proposed that RolR may represent a new subfamily of TetR proteins that are invovled in aromatic degradation and sharing common recognition mode as for RolR.

PubMed: 21559286
DOI: 10.1371/journal.pone.0019529

Experimental method

X-RAY DIFFRACTION (2.5 Å)