Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2050311 | FEBS Letters | 2006 | 6 Pages |
Abstract
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.
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Authors
Yarden Opatowsky, Yehezkel Sasson, Isabella Shaked, Yvona Ward, Orna Chomsky-Hecht, Yael Litvak, Zvi Selinger, Kathleen Kelly, Joel A. Hirsch,