2XAO
Inositol 1,3,4,5,6-pentakisphosphate 2-kinase from A. thaliana in complex with IP5
2XAO の概要
| エントリーDOI | 10.2210/pdb2xao/pdb |
| 関連するPDBエントリー | 2XAL 2XAM 2XAN 2XAR |
| 分子名称 | INOSITOL-PENTAKISPHOSPHATE 2-KINASE, MYO-INOSITOL-(1,3,4,5,6)-PENTAKISPHOSPHATE, ZINC ION (3 entities in total) |
| 機能のキーワード | transferase, inositol polyphosphate kinase, phytic acid synthase |
| 由来する生物種 | Arabidopsis thaliana (THALE CRESS) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 102726.10 |
| 構造登録者 | Gonzalez, B.,Banos-Sanz, J.I.,Villate, M.,Brearley, C.A.,Sanz-Aparicio, J. (登録日: 2010-03-31, 公開日: 2010-05-19, 最終更新日: 2023-12-20) |
| 主引用文献 | Gonzalez, B.,Banos-Sanz, J.I.,Villate, M.,Brearley, C.A.,Sanz-Aparicio, J. 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. Proc.Natl.Acad.Sci.USA, 107:9608-, 2010 Cited by PubMed Abstract: Inositol phosphates (InsPs) are signaling molecules with multiple roles in cells. In particular (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. PubMed: 20453199DOI: 10.1073/PNAS.0912979107 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.9 Å) |
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