3O1H

Crystal Structure of the TorS sensor domain - TorT complex in the presence of TMAO

Summary for 3O1H

• Entry DOI: 10.2210/pdb3o1h/pdb
• Related: 3I9W 3I9Y 3O1I 3O1J
• Descriptor: Sensor protein TorS, Periplasmic protein TorT, trimethylamine oxide, ... (4 entities in total)
• Functional Keywords: tmao bound, two component sensor, periplasmic binding protein, tmao binding, signaling protein
• Biological source: Vibrio parahaemolyticus; More
• Total number of polymer chains: 2
• Total formula weight: 65664.16

Authors

Moore, J.O.,Hendrickson, W.A. (deposition date: 2010-07-21, release date: 2011-12-21, Last modification date: 2024-10-09)

Primary citation

Moore, J.O.,Hendrickson, W.A.
An asymmetry-to-symmetry switch in signal transmission by the histidine kinase receptor for TMAO.
Structure, 20:729-741, 2012

PubMed Abstract: 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.

PubMed: 22483119
DOI: 10.1016/j.str.2012.02.021

Experimental method

X-RAY DIFFRACTION (3.1 Å)