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Structural and functional analysis of a truncated form of Saccharomyces cerevisiae ATP sulfurylase: C-terminal domain essential for oligomer formation but not for activity.

Lalor DJ, Schnyder T, Saridakis V, Pilloff DE, Dong A, Tang H, Leyh TS, Pai EF
Protein Eng 16 1071-9 (2003)
Cited: 10 times
EuropePMC logo PMID: 14983089

Abstract

ATP sulfurylase catalyzes the first step in the activation of sulfate by transferring the adenylyl-moiety (AMP approximately ) of ATP to sulfate to form adenosine 5'-phosphosulfate (APS) and pyrophosphate (PP(i)). Subsequently, APS kinase mediates transfer of the gamma-phosphoryl group of ATP to APS to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS) and ADP. The recently determined crystal structure of yeast ATP sulfurylase suggests that its C-terminal domain is structurally quite independent from the other domains, and not essential for catalytic activity. It seems, however, to dictate the oligomerization state of the protein. Here we show that truncation of this domain results in a monomeric enzyme with slightly enhanced catalytic efficiency. Structural alignment of the C-terminal domain indicated that it is extremely similar in its fold to APS kinase although not catalytically competent. While carrying out these structural and functional studies a surface groove was noted. Careful inspection and modeling revealed that the groove is sufficiently deep and wide, as well as properly positioned, to act as a substrate channel between the ATP sulfurylase and APS kinase-like domains of the enzyme.

Reviews citing this publication (2)

  1. Adenosine-5'-phosphosulfate--a multifaceted modulator of bifunctional 3'-phospho-adenosine-5'-phosphosulfate synthases and related enzymes. Mueller JW, Shafqat N. FEBS J 280 3050-3057 (2013)
  2. Diversity and regulation of ATP sulfurylase in photosynthetic organisms. Prioretti L, Gontero B, Hell R, Giordano M. Front Plant Sci 5 597 (2014)

Articles citing this publication (8)

  1. Molecular basis for G protein control of the prokaryotic ATP sulfurylase. Mougous JD, Lee DH, Hubbard SC, Schelle MW, Vocadlo DJ, Berger JM, Bertozzi CR. Mol Cell 21 109-122 (2006)
  2. Crystal structure of the bifunctional ATP sulfurylase-APS kinase from the chemolithotrophic thermophile Aquifex aeolicus. Yu Z, Lansdon EB, Segel IH, Fisher AJ. J Mol Biol 365 732-743 (2007)
  3. Complex formation between recombinant ATP sulfurylase and APS reductase of Allium cepa (L.). Cumming M, Leung S, McCallum J, McManus MT. FEBS Lett 581 4139-4147 (2007)
  4. Sulfate activation enzymes: phylogeny and association with pyrophosphatase. Bradley ME, Rest JS, Li WH, Schwartz NB. J Mol Evol 68 1-13 (2009)
  5. An alternative assay to discover potential calmodulin inhibitors using a human fluorophore-labeled CaM protein. González-Andrade M, Figueroa M, Rodríguez-Sotres R, Mata R, Sosa-Peinado A. Anal Biochem 387 64-70 (2009)
  6. Cloning, expression and bioinformatics analysis of ATP sulfurylase from Acidithiobacillus ferrooxidans ATCC 23270 in Escherichia coli. Jaramillo ML, Abanto M, Quispe RL, Calderón J, Del Valle LJ, Talledo M, Ramírez P. Bioinformation 8 695-704 (2012)
  7. Designing Cyclic-Constrained Peptides to Inhibit Human Phosphoglycerate Dehydrogenase. Qing X, Wang Q, Xu H, Liu P, Lai L. Molecules 28 6430 (2023)
  8. Purification, crystallization and preliminary X-ray diffraction analysis of adenosine triphosphate sulfurylase (ATPS) from the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774. Gavel OY, Kladova AV, Bursakov SA, Dias JM, Texeira S, Shnyrov VL, Moura JJ, Moura I, Romão MJ, Trincão J. Acta Crystallogr Sect F Struct Biol Cryst Commun 64 593-595 (2008)


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