Molecular Basis for G Protein Control of the Prokaryotic ATP Sulfurylase
| Autor: | Carolyn R. Bertozzi, Sarah C. Hubbard, David J. Vocadlo, James M. Berger, Michael W. Schelle, Joseph D. Mougous, Dong H. Lee |
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| Rok vydání: | 2006 |
| Předmět: |
Models
Molecular GTP' G protein Protein subunit Molecular Sequence Data Pseudomonas syringae GTPase Biology Crystallography X-Ray 03 medical and health sciences Bacterial Proteins GTP-Binding Proteins Humans Nucleotide Amino Acid Sequence Sulfate assimilation Molecular Biology Adenylylation 030304 developmental biology chemistry.chemical_classification 0303 health sciences Molecular Structure Sulfates 030302 biochemistry & molecular biology Cell Biology Sulfate Adenylyltransferase Protein Structure Tertiary Biochemistry chemistry G-domain Guanosine Triphosphate Dimerization Sequence Alignment |
| Zdroj: | Molecular Cell. 21:109-122 |
| ISSN: | 1097-2765 |
| DOI: | 10.1016/j.molcel.2005.10.034 |
| Popis: | Summary Sulfate assimilation is a critical component of both primary and secondary metabolism. An essential step in this pathway is the activation of sulfate through adenylation by the enzyme ATP sulfurylase (ATPS), forming adenosine 5′-phosphosulfate (APS). Proteobacterial ATPS overcomes this energetically unfavorable reaction by associating with a regulatory G protein, coupling the energy of GTP hydrolysis to APS formation. To discover the molecular basis of this unusual role for a G protein, we biochemically characterized and solved the X-ray crystal structure of a complex between Pseudomonas syringae ATPS (CysD) and its associated regulatory G protein (CysN). The structure of CysN•D shows the two proteins in tight association; however, the nucleotides bound to each subunit are spatially segregated. We provide evidence that conserved switch motifs in the G domain of CysN allosterically mediate interactions between the nucleotide binding sites. This structure suggests a molecular mechanism by which conserved G domain architecture is used to energetically link GTP turnover to the production of an essential metabolite. |
| Databáze: | OpenAIRE |
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