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Inositol 1,3,4,5,6-pentakisphosphate 2-kinase is a distant IPK member with a singular inositide binding site for axial 2-OH recognition

Beatriz González, Jose Ignacio Baños-Sanz, Maider Villate, Charles Alistair Brearley, Julia Sanz-Aparicio and Susan S. Taylor
Proceedings of the National Academy of Sciences of the United States of America
Vol. 107, No. 21 (May 25, 2010), pp. 9608-9613
Stable URL: http://www.jstor.org/stable/25681647
Page Count: 6
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Inositol 1,3,4,5,6-pentakisphosphate 2-kinase is a distant IPK member with a singular inositide binding site for axial 2-OH recognition
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Abstract

Inositol phosphates (InsPs) are signaling molecules with multiple roles in cells. In particular Ins(1,2,3,4,5,6)P₆ (InsP₆) is involved in mRNA export and editing or chromatin remodeling among other events. InsP₆ accumulates as mixed salts (phytate) in storage tissues of plants and plays a key role in their physiology. Human diets that are exclusively grain-based provide an excess of InsP₆ that, through chelation of metal ions, may have a detrimental effect on human health. Ins(1,3,4,5,6)P₅ 2-kinase (InsP₅ 2-kinase or Ipk1) catalyses the synthesis of InsP₆ from InsP₅ and ATP, and is the only enzyme that transfers a phosphate group to the axial 2-OH of the myo-inositide. We present the first structure for an InsP₅ 2-kinase in complex with both substrates and products. This enzyme presents a singular structural region for inositide binding that encompasses almost half of the protein. The key residues in substrate binding are identified, with Asp368 being responsible for recognition of the axial 2-OH. This study sheds light on the unique molecular mechanism for the synthesis of the precursor of inositol pyrophosphates.

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