2HT6

Crystal structure of Human Gem G-domain bound to GDP

Summary for 2HT6

• Entry DOI: 10.2210/pdb2ht6/pdb
• Descriptor: GTP-binding protein GEM, MAGNESIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: small g-protein, signaling protein
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane; Peripheral membrane protein; Cytoplasmic side: P55040
• Total number of polymer chains: 2
• Total formula weight: 40159.39

Authors

Opatowsky, Y.,Hirsch, J.A. (deposition date: 2006-07-25, release date: 2006-10-31, Last modification date: 2024-02-14)

Primary citation

Opatowsky, Y.,Sasson, Y.,Shaked, I.,Ward, Y.,Chomsky-Hecht, O.,Litvak, Y.,Selinger, Z.,Kelly, K.,Hirsch, J.A.
Structure-function studies of the G-domain from human gem, a novel small G-protein.
Febs Lett., 580:5959-5964, 2006

PubMed 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 A 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.

PubMed: 17052716
DOI: 10.1016/j.febslet.2006.09.067

Experimental method

X-RAY DIFFRACTION (2.4 Å)