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Gonzalez, Beatriz, Banos-Sanz, Jose Ignacio, Villate, Maider, Brearley, Charles Alistair 
ORCID: https://orcid.org/0000-0001-6179-9109 and Sanz-Aparicio, Julia
(2010)
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.
Proceedings of the National Academy of Sciences, 107 (21).
pp. 9608-9613.
ISSN 1091-6490
Abstract
Inositol phosphates (InsPs) are signaling molecules with multiple roles in cells. In particular Graphic (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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | sdg 3 - good health and well-being ,/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_being |
| Faculty \ School: | Faculty of Science > School of Biological Sciences |
| UEA Research Groups: | Faculty of Science > Research Groups > Plant Sciences Faculty of Science > Research Groups > Molecular Microbiology |
| Related URLs: | |
| Depositing User: | EPrints Services |
| Date Deposited: | 01 Oct 2010 13:38 |
| Last Modified: | 24 Sep 2024 09:09 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/1674 |
| DOI: | 10.1073/pnas.0912979107 |
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