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New Insights on Signal Propagation by Sensory Rhodopsin II/Transducer Complex.

A Ishchenko1,2, E Round1,3, V Borshchevskiy1,4

  • 1Institute of Complex Systems (ICS), ICS-6: Structural Biochemistry, Research Centre Jülich, 52425 Jülich, Germany.

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|February 7, 2017
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Halobacteria use sensory rhodopsin II (NpSRII) and transducer (NpHtrII) for negative phototaxis. Crystal structures reveal distinct "U"-shaped and "V"-shaped conformations, suggesting a role in signal transduction.

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biophysics

Background:

  • Sensory rhodopsin II (NpSRII) and its transducer (NpHtrII) form a complex in halobacteria.
  • This complex mediates negative phototaxis, a light-guided behavioral response.
  • The signaling mechanism is analogous to eubacterial two-component chemotaxis systems.

Purpose of the Study:

  • To determine the crystal structures of the NpSRII/NpHtrII complex in its ground and active M-states.
  • To investigate the structural basis of signal transduction in this photo-sensory system.

Main Methods:

  • X-ray crystallography was used to obtain structures in the I212121 space group.
  • Computer modeling was employed to analyze the HAMP domain interactions in different conformations.

Main Results:

  • Two distinct conformations, a parallel "U"-shape and a gusset-like "V"-shape, were observed for the NpSRII/NpHtrII complex.
  • Monomer structures were similar, but dimer orientations differed significantly from previous P212121 space group findings.
  • "U"-shaped conformation shows optimal HAMP domain interactions, supporting its role in the ground state.

Conclusions:

  • The "U"-shaped structure likely represents the biologically relevant ground state.
  • "V"-shaped structure may represent the active state.
  • Conformational change from "U" to "V" is proposed as the mechanism for signal transduction from the receptor to the transducer's signaling domain.