Molecular basis for G protein control of the prokaryotic ATP sulfurylase.

Content Provider	Semantic Scholar
Author	Mougous, Joseph D. Lee, Dong Ha Hubbard, S. Catherine Schelle, Michael W. Vocadlo, David J. Berger, James M. Bertozzi, Carolyn R.
Copyright Year	2006
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.
Starting Page	29
Ending Page	31
Page Count	3
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://faculty.washington.edu/mougous/wp-content/uploads/2012/02/Mougous_2006_3.pdf
PubMed reference number	16387658v1
Volume Number	21
Issue Number	1
Journal	Molecular cell
Language	English
Access Restriction	Open
Subject Keyword	Adenosine Phosphosulfate Adenosine Triphosphate Binding Sites Guanosine Triphosphate Nucleotides Secondary Metabolism Sulfate Adenylyltransferase nucleotide binding
Content Type	Text
Resource Type	Article