Molecular basis for G protein control of the prokaryotic ATP sulfurylase

Joseph D. Mougous, Dong H. Lee, Sarah C. Hubbard, Michael W. Schelle, David J. Vocadlo, James M. Berger, Carolyn R. Bertozzi

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish (US)
Pages (from-to)109-122
Number of pages14
JournalMolecular cell
Volume21
Issue number1
DOIs
StatePublished - Jan 6 2006

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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