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Nucleotide dependent cysteine reactivity of hGBP1 uncovers a domain movement during GTP hydrolysis
Author(s) -
Vöpel Tobias,
Kunzelmann Simone,
Herrmann Christian
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.05.027
Subject(s) - gtpase , gtp' , cysteine , nucleotide , chemistry , dynamin , biochemistry , cyclic nucleotide binding domain , guanine nucleotide exchange factor , hydrolysis , biophysics , stereochemistry , biology , enzyme , receptor , endocytosis , gene
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.