Nucleotide dependent cysteine reactivity of hGBP1 uncovers a domain movement during GTP hydrolysis
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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
Published on: June 7, 2018
Tobias Vöpel1, Simone Kunzelmann, Christian Herrmann
1Physikalische Chemie I, Fakultät für Chemie und Biochemie, Ruhr-Universität Bochum, 44780 Bochum, Germany.
Abstract:
As a member of the dynamin superfamily human guanylate-binding protein 1 (hGBP1) binds and hydrolyses GTP thereby undergoing structural changes which lead to self-assembly of the protein. Here, we employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of accessibility by the compound after addition of GTP. Our results indicate that nucleotide hydrolysis induces a domain movement in hGBP1, which we suggest enables further assembly of the protein.
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