2XAN
inositol 1,3,4,5,6-pentakisphosphate 2-kinase from A. thaliana in complex with AMP PNP and IP5
Summary for 2XAN
Entry DOI | 10.2210/pdb2xan/pdb |
Related | 2XAL 2XAM 2XAO 2XAR |
Descriptor | INOSITOL-PENTAKISPHOSPHATE 2-KINASE, MYO-INOSITOL-(1,3,4,5,6)-PENTAKISPHOSPHATE, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (6 entities in total) |
Functional Keywords | transferase, phytic acid synthase, ip6 |
Biological source | Arabidopsis thaliana (THALE CRESS) |
Total number of polymer chains | 2 |
Total formula weight | 103787.10 |
Authors | Gonzalez, B.,Banos-Sanz, J.I.,Villate, M.,Brearley, C.A.,Sanz-Aparicio, J. (deposition date: 2010-03-31, release date: 2010-05-19, Last modification date: 2023-12-20) |
Primary citation | 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 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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