期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 107, 期 21, 页码 9608-9613出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0912979107
关键词
InsP5 2-kinase; IP5; IP6; ipk1; crystal structure
资金
- Ramon y Cajal [RYC-2006-002701]
- Ministerio de Educacion [AP2008-00916]
- Biotechnology and Biological Sciences Research Council of the UK [BB/C514090/1]
- Comunidad de Madrid-CSIC [CCG07-CSIC/GEN-2232, CCG08-CSIC/GEN-3490]
- Ministerio de Ciencia e Innovacion [BFU2008-02897/BMC]
- Ministerio de Educacion y Ciencia [RYC-2006-002701]
- Biotechnology and Biological Sciences Research Council [BB/C514090/1] Funding Source: researchfish
Inositol phosphates (InsPs) are signaling molecules with multiple roles in cells. In particular Ins(1,2,3,4,5,6)P-6 (InsP(6)) is involved in mRNA export and editing or chromatin remodeling among other events. InsP(6) 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 InsP(6) that, through chelation of metal ions, may have a detrimental effect on human health. Ins(1,3,4,5,6)P-5 2-kinase (InsP(5) 2-kinase or Ipk1) catalyses the synthesis of InsP(6) from InsP(5) 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 InsP(5) 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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