The crystal structure of a self-activating g protein α subunit reveals its distinct mechanism of signal initiation

Science Signaling

Volumn 4, Issue 159, 2011, Pages

  Jones, Janice C ^a   Duffy, Jeffrey W ^a   Machius, Mischa ^a,b   Temple, Brenda R S ^a,b   Dohlman, Henrik G ^a   Jones, Alan M ^a,b  

^a UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF NORTH CAROLINA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN ALPHA; G PROTEIN COUPLED RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; PROTEIN SUBUNIT; UNCLASSIFIED DRUG; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ARABIDOPSIS PROTEIN; GPA1 PROTEIN, ARABIDOPSIS; GUANINE NUCLEOTIDE BINDING PROTEIN ALPHA SUBUNIT; GUANINE NUCLEOTIDE EXCHANGE FACTOR;

ARABIDOPSIS; ARTICLE; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STABILITY; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; CRYSTALLIZATION; GENETICS; KINETICS; METABOLISM; MOLECULAR GENETICS; MUTATION; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; X RAY DIFFRACTION;

ANIMALIA; ARABIDOPSIS; ARABIDOPSIS THALIANA;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; ARABIDOPSIS PROTEINS; CIRCULAR DICHROISM; CRYSTALLIZATION; GTP-BINDING PROTEIN ALPHA SUBUNITS; GUANINE NUCLEOTIDE EXCHANGE FACTORS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, G-PROTEIN-COUPLED; SEQUENCE HOMOLOGY, AMINO ACID; SIGNAL TRANSDUCTION; X-RAY DIFFRACTION;

EID: 79851474025     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.2001446     Document Type: Article

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31. Acknowledgments: We thank J. Vanhooke for valuable help throughout the crystallization process, B. Wallace and M. Miley for collecting diffraction data, A. Tripathy (University of North Carolina Macromolecular Interactions Facility) for instruction in CD spectroscopy, and J. Sondek for sharing equipment and insightful comments on the manuscript. Funding: This work was supported by grants from the National Institutes of General Medical Sciences (NIGMS) (R01GM065989), Department of Energy (DE-FG02-05er15671), and National Science Foundation (MCB-0723515 and MCB-0718202) to A.M.J. and NIGMS (R01GM080739) to H.G.D. J.C.J. was supported by a Ruth L. Kirschstein postdoctoral award. Author contributions: J.C.J. managed the project, made reagents, designed the experiments, acquired and analyzed the data, and wrote the manuscript; J.W.D. made reagents, acquired and analyzed the data, and crystallized the protein; M.M. solved the crystal structure, analyzed the data, and wrote the manuscript; B.R.S.T. designed the experiments, acquired and analyzed the data, and wrote the manuscript; H.G.D. and A.M.J. analyzed the data, managed the project, and wrote the manuscript. Competing interests: The authors declare that they have no competing interests. Accession numbers: Structure coordinates for AtGPA1 are deposited in the Protein Data Bank (www.pdb.org) as 2XTZ.