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- W2135489056 abstract "FixJ is a two-domain response regulator involved in nitrogen fixation in Sinorhizobium meliloti. Recent X-ray characterization of both the native (unphosphorylated) and the active (phosphorylated) states of the protein identify conformational changes of the beta4-alpha4 loop and the conserved residue Phe101 as the key switches in activation. These structures also allowed investigation of the transition between conformations of this two-component regulatory receiver domain by molecular dynamics simulations. The path for the conformational change was studied with a distance constraint directing the system from one state to the other. The simulations provide evidence for a correlation between the conformation of the beta4-alpha4 loop and the orientation of the residue Phe101. A model presenting the sequence of events during the activation/deactivation process is discussed." @default.
- W2135489056 created "2016-06-24" @default.
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- W2135489056 date "2002-11-01" @default.
- W2135489056 modified "2023-10-10" @default.
- W2135489056 title "Molecular dynamics of the FixJ receiver domain: movement of the β4-α4 loop correlates with the in and out flip of Phe101" @default.
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- W2135489056 doi "https://doi.org/10.1110/ps.0218802" @default.
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