3aqt

CRYSTAL STRUCTURE OF RolR (NCGL1110) complex WITH ligand RESORCINOL

spinqualitylabelsall models 3aqt, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3aqt is a 2 chain structure with sequence from Corynebacterium glutamicum ATCC 13032. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: MSE, RCO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8NR95_CORGL Publication Abstract from PubMed 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 A and 3.6 A, 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 A to 30.4 A. 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. Crystal structures of the transcriptional repressor RolR reveals a novel recognition mechanism between inducer and regulator.,Li DF, Zhang N, Hou YJ, Huang Y, Hu Y, Zhang Y, Liu SJ, Wang DC PLoS One. 2011 May 3;6(5):e19529. PMID:21559286 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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