Document Detail


Molecular basis for G protein control of the prokaryotic ATP sulfurylase.
MedLine Citation:
PMID:  16387658     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Joseph D Mougous; Dong H Lee; Sarah C Hubbard; Michael W Schelle; David J Vocadlo; James M Berger; Carolyn R Bertozzi
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural    
Journal Detail:
Title:  Molecular cell     Volume:  21     ISSN:  1097-2765     ISO Abbreviation:  Mol. Cell     Publication Date:  2006 Jan 
Date Detail:
Created Date:  2006-01-02     Completed Date:  2006-02-27     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  9802571     Medline TA:  Mol Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  109-22     Citation Subset:  IM    
Affiliation:
Howard Hughes Medical Institute, University of California, Berkeley, Berkeley, California 94720, USA.
Data Bank Information
Bank Name/Acc. No.:
PDB/1ZUN
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Bacterial Proteins / chemistry*,  genetics,  metabolism
Crystallography, X-Ray
Dimerization
GTP-Binding Proteins / genetics,  metabolism*
Guanosine Triphosphate / metabolism
Humans
Models, Molecular
Molecular Sequence Data
Molecular Structure
Protein Structure, Tertiary*
Pseudomonas syringae / enzymology*,  genetics
Sequence Alignment
Sulfate Adenylyltransferase / chemistry*,  genetics,  metabolism
Sulfates / metabolism*
Grant Support
ID/Acronym/Agency:
AI51622/AI/NIAID NIH HHS; P50-GM62410/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Sulfates; 86-01-1/Guanosine Triphosphate; EC 2.7.7.4/Sulfate Adenylyltransferase; EC 3.6.1.-/GTP-Binding Proteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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