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FEBS Lett. 2009 Jun 18;583(12):1923-7. doi: 10.1016/j.febslet.2009.05.027. Epub 2009 May 20.

Nucleotide dependent cysteine reactivity of hGBP1 uncovers a domain movement during GTP hydrolysis.

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  • 1Physikalische Chemie I, Fakultät für Chemie und Biochemie, Ruhr-Universität Bochum, 44780 Bochum, Germany.


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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