3o1i

Crystal Structure of the TorS sensor domain - TorT complex in the absence of ligand

spinqualitylabelsall models 3o1i, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3o1i is a 4 chain structure with sequence from Vibrio parahaemolyticus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: PE4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q87ID1_VIBPA Publication Abstract from PubMed The osmoregulator trimethylamine-N-oxide (TMAO), commonplace in aquatic organisms, is used as the terminal electron acceptor for respiration in many bacterial species. The TMAO reductase (Tor) pathway for respiratory catalysis is controlled by a receptor system that comprises the TMAO-binding protein TorT, the sensor histidine kinase TorS, and the response regulator TorR. Here we study the TorS/TorT sensor system to gain mechanistic insight into signaling by histidine kinase receptors. We determined crystal structures for complexes of TorS sensor domains with apo TorT and with TorT (TMAO); we characterized TorS sensor associations with TorT in solution; we analyzed the thermodynamics of TMAO binding to TorT-TorS complexes; and we analyzed in vivo responses to TMAO through the TorT/TorS/TorR system to test structure-inspired hypotheses. TorS-TorT(apo) is an asymmetric 2:2 complex that binds TMAO with negative cooperativity to form a symmetric active kinase. An asymmetry-to-symmetry switch in signal transmission by the histidine kinase receptor for TMAO.,Moore JO, Hendrickson WA Structure. 2012 Apr 4;20(4):729-41. Epub 2012 Apr 3. PMID:22483119 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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