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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Amino Acid Substitution
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Animals
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COS Cells
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Chlorocebus aethiops
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Crystallography, X-Ray
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Guanosine Diphosphate / metabolism
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Guanosine Triphosphate / metabolism
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Humans
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In Vitro Techniques
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Intracellular Signaling Peptides and Proteins / genetics
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Intracellular Signaling Peptides and Proteins / metabolism
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Models, Molecular
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Molecular Sequence Data
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Monomeric GTP-Binding Proteins / chemistry*
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Monomeric GTP-Binding Proteins / genetics
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Monomeric GTP-Binding Proteins / metabolism*
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Mutagenesis, Site-Directed
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Protein Serine-Threonine Kinases / genetics
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Protein Serine-Threonine Kinases / metabolism
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Protein Structure, Tertiary
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Sequence Homology, Amino Acid
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Static Electricity
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rho-Associated Kinases
Substances
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Intracellular Signaling Peptides and Proteins
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Recombinant Proteins
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Guanosine Diphosphate
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Guanosine Triphosphate
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Protein Serine-Threonine Kinases
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rho-Associated Kinases
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GEM protein, human
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Monomeric GTP-Binding Proteins