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Metaphosphate in the active site of fructose-1,6-bisphosphatase.

Choe JY, Iancu CV, Fromm HJ, Honzatko RB
J Biol Chem 278 16015-20 (2003)
Related entries: 1nux, 1nuy

Cited: 12 times
EuropePMC logo PMID: 12595528

Abstract

The hydrolysis of a phosphate ester can proceed through an intermediate of metaphosphate (dissociative mechanism) or through a trigonal bipryamidal transition state (associative mechanism). Model systems in solution support the dissociative pathway, whereas most enzymologists favor an associative mechanism for enzyme-catalyzed reactions. Crystals of fructose-1,6-bisphosphatase grow from an equilibrium mixture of substrates and products at near atomic resolution (1.3 A). At neutral pH, products of the reaction (orthophosphate and fructose 6-phosphate) bind to the active site in a manner consistent with an associative reaction pathway; however, in the presence of inhibitory concentrations of K+ (200 mm), or at pH 9.6, metaphosphate and water (or OH-) are in equilibrium with orthophosphate. Furthermore, one of the magnesium cations in the pH 9.6 complex resides in an alternative position, and suggests the possibility of metal cation migration as the 1-phosphoryl group of the substrate undergoes hydrolysis. To the best of our knowledge, the crystal structures reported here represent the first direct observation of metaphosphate in a condensed phase and may provide the structural basis for fundamental changes in the catalytic mechanism of fructose-1,6-bisphosphatase in response to pH and different metal cation activators.

Articles - 1nuw mentioned but not cited (2)

  1. Crystal structures of human muscle fructose-1,6-bisphosphatase: novel quaternary states, enhanced AMP affinity, and allosteric signal transmission pathway. Shi R, Chen ZY, Zhu DW, Li C, Shan Y, Xu G, Lin SX. PLoS One 8 e71242 (2013)
  2. Activation of a nucleotide-dependent RCK domain requires binding of a cation cofactor to a conserved site. Teixeira-Duarte CM, Fonseca F, Morais-Cabral JH. Elife 8 e50661 (2019)


Reviews citing this publication (2)

  1. Mechanism and applications of phosphite dehydrogenase. Relyea HA, van der Donk WA. Bioorg Chem 33 171-189 (2005)
  2. Phosphoryl transfer by aminoglycoside 3'-phosphotransferases and manifestation of antibiotic resistance. Kim C, Mobashery S. Bioorg Chem 33 149-158 (2005)

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  1. Alkaline phosphatase mono- and diesterase reactions: comparative transition state analysis. Zalatan JG, Herschlag D. J Am Chem Soc 128 1293-1303 (2006)
  2. The first crystal structure of the novel class of fructose-1,6-bisphosphatase present in thermophilic archaea. Nishimasu H, Fushinobu S, Shoun H, Wakagi T. Structure 12 949-959 (2004)
  3. Description of pentacoordinated phosphorus under an external electric field: which basis sets and semi-empirical methods are needed? Marcos E, Anglada JM, Crehuet R. Phys Chem Chem Phys 10 2442-2450 (2008)
  4. Mechanism of displacement of a catalytically essential loop from the active site of mammalian fructose-1,6-bisphosphatase. Gao Y, Iancu CV, Mukind S, Choe JY, Honzatko RB. Biochemistry 52 5206-5216 (2013)
  5. A structural exposé of noncanonical molecular reactivity within the protein tyrosine phosphatase WPD loop. Wang H, Perera L, Jork N, Zong G, Riley AM, Potter BVL, Jessen HJ, Shears SB. Nat Commun 13 2231 (2022)
  6. Quadruple space-group ambiguity owing to rotational and translational noncrystallographic symmetry in human liver fructose-1,6-bisphosphatase. Ruf A, Tetaz T, Schott B, Joseph C, Rudolph MG. Acta Crystallogr D Struct Biol 72 1212-1224 (2016)
  7. Quantum Mechanical/Molecular Mechanical Analysis of the Catalytic Mechanism of Phosphoserine Phosphatase. Krachtus D, Smith JC, Imhof P. Molecules 23 E3342 (2018)
  8. Identification of a potential proton donor to the linking oxygen atom in a three-metal ion assisted catalysis pathway catalyzed by Fructose-1, 6-bisphosphatase. Wang J, Wang Z, Ling B, Cao N, Wang W. J Mol Graph Model 73 191-199 (2017)


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