5kbh | pdb_00005kbh

CRYSTAL STRUCTURE OF THE AROMATIC SENSOR DOMAIN OF MOPR IN COMPLEX WITH 3-CHLORO-PHENOL

spinqualitylabelsall models 5kbh, resolution 2.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5kbh is a 2 chain structure with sequence from Acinetobacter calcoaceticus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.55Å Ligands: 3CH, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MOPR_ACIGI Involved in the regulation of the phenol degradation pathway. Activates phenol hydroxylase expression in the presence of phenol. Publication Abstract from PubMed Phenol and its derivatives are common pollutants that are present in industrial discharge and are major xenobiotics that lead to water pollution. To monitor as well as improve water quality, attempts have been made in the past to engineer bacterial in vivo biosensors. However, due to the paucity of structural information, there is insufficiency in gauging the factors that lead to high sensitivity and selectivity, thereby impeding development. Here, we present the crystal structure of the sensor domain of MopR (MopRAB) from Acinetobacter calcoaceticus in complex with phenol and its derivatives to a maximum resolution of 2.5 A. The structure reveals that the N-terminal residues 21-47 possess a unique fold, which are involved in stabilization of the biological dimer, and the central ligand binding domain belongs to the "nitric oxide signaling and golgi transport" fold, commonly present in eukaryotic proteins that bind long-chain fatty acids. In addition, MopRAB nests a zinc atom within a novel zinc binding motif, crucial for maintaining structural integrity. We propose that this motif is crucial for orchestrated motions associated with the formation of the effector binding pocket. Our studies reveal that residues W134 and H106 play an important role in ligand binding and are the key selectivity determinants. Furthermore, comparative analysis of MopR with XylR and DmpR sensor domains enabled the design of a MopR binding pocket that is competent in binding DmpR-specific ligands. Collectively, these findings pave way towards development of specific/broad based biosensors, which can act as useful tools for detection of this class of pollutants. Structural Basis of Selective Aromatic Pollutant Sensing by the Effector Binding Domain of MopR, an NtrC Family Transcriptional Regulator.,Ray S, Gunzburg MJ, Wilce M, Panjikar S, Anand R ACS Chem Biol. 2016 Jun 30. PMID:27362503 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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