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The linker pivot in Ci-VSP: the key to unlock catalysis.
Zitatschlüssel Hobiger2013
Autor Hobiger, Kirstin and Utesch, Tillmann and Mroginski, Maria Andrea and Seebohm, Guiscard and Friedrich, Thomas
Seiten e70272
Jahr 2013
DOI 10.1371/journal.pone.0070272
Journal PLoS One
Jahrgang 8
Nummer 7
Institution Institute of Chemistry, Max-Volmer-Laboratory of Biophysical Chemistry, Technische Universität Berlin, Berlin, Germany. kirstin.hobiger@tu-berlin.de
Zusammenfassung In the voltage-sensitive phosphatase Ci-VSP, conformational changes in the transmembrane voltage sensor domain (VSD) are transduced to the intracellular catalytic domain (CD) leading to its dephosphorylation activity against membrane-embedded phosphoinositides. The linker between both domains is proposed to be crucial for the VSD-CD coupling. With a combined approach of electrophysiological measurements on Xenopus oocytes and molecular dynamics simulations of a Ci-VSP model embedded in a lipid bilayer, we analyzed how conformational changes in the linker mediate the interaction between the CD and the activated VSD. In this way, we identified specific residues in the linker that interact with well-defined amino acids in one of the three loops forming the active site of the protein, named TI loop. With our results, we shed light into the early steps of the coupling process between the VSD and the CD, which are based on fine-tuned electrostatic and hydrophobic interactions between the linker, the membrane and the CD.
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