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Structure–function studies of the G‐domain from human gem, a novel small G‐protein
Author(s) -
Opatowsky Yarden,
Sasson Yehezkel,
Shaked Isabella,
Ward Yvona,
Chomsky-Hecht Orna,
Litvak Yael,
Selinger Zvi,
Kelly Kathleen,
Hirsch Joel A.
Publication year - 2006
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.2006.09.067
Subject(s) - gtp' , subfamily , chemistry , domain (mathematical analysis) , nucleotide , function (biology) , sequence (biology) , biology , computational biology , biochemistry , stereochemistry , biophysics , microbiology and biotechnology , gene , enzyme , mathematical analysis , mathematics
Gem, a member of the Rad,Gem/Kir subfamily of small G‐proteins, has unique sequence features. We report here the crystallographic structure determination of the Gem G‐domain in complex with nucleotide to 2.4 Å resolution. Although the basic Ras protein fold is maintained, the Gem switch regions emphatically differ from the Ras paradigm. Our ensuing biochemical characterization indicates that Gem G‐domain markedly prefers GDP over GTP. Two known functions of Gem are distinctly affected by spatially separated clusters of mutations.