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2XAR

Inositol 1,3,4,5,6-pentakisphosphate 2-kinase from A. thaliana in complex with IP6.

Summary for 2XAR
Entry DOI10.2210/pdb2xar/pdb
Related2XAL 2XAM 2XAN 2XAO
DescriptorINOSITOL-PENTAKISPHOSPHATE 2-KINASE, INOSITOL HEXAKISPHOSPHATE, ZINC ION (3 entities in total)
Functional Keywordstransferase, ipk, insp5 2-k, phytic acid synthase
Biological sourceArabidopsis thaliana (THALE CRESS)
Total number of polymer chains2
Total formula weight102886.06
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 citationGonzalez, 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: 20453199
DOI: 10.1073/PNAS.0912979107
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.1 Å)
Structure validation

227933

数据于2024-11-27公开中

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