1Z2O

Inositol 1,3,4-trisphosphate 5/6-Kinase in complex with mg2+/ADP/Ins(1,3,4,6)P4

1Z2O の概要

• エントリーDOI: 10.2210/pdb1z2o/pdb
• 関連するPDBエントリー: 1Z2N 1Z2P
• 分子名称: inositol 1,3,4-trisphosphate 5/6-kinase, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: inositol phosphate kinase, atp-grasp, transferase
• 由来する生物種: Entamoeba histolytica
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37912.33

構造登録者

Miller, G.J.,Wilson, M.P.,Majerus, P.W.,Hurley, J.H. (登録日: 2005-03-08, 公開日: 2005-04-19, 最終更新日: 2024-02-14)

主引用文献

Miller, G.J.,Wilson, M.P.,Majerus, P.W.,Hurley, J.H.
Specificity determinants in inositol polyphosphate synthesis: crystal structure of inositol 1,3,4-trisphosphate 5/6-kinase.
Mol.Cell, 18:201-212, 2005

PubMed Abstract: Inositol hexakisphosphate and other inositol high polyphosphates have diverse and critical roles in eukaryotic regulatory pathways. Inositol 1,3,4-trisphosphate 5/6-kinase catalyzes the rate-limiting step in inositol high polyphosphate synthesis in animals. This multifunctional enzyme also has inositol 3,4,5,6-tetrakisphosphate 1-kinase and other activities. The structure of an archetypal family member, from Entamoeba histolytica, has been determined to 1.2 A resolution in binary and ternary complexes with nucleotide, substrate, and product. The structure reveals an ATP-grasp fold. The inositol ring faces ATP edge-on such that the 5- and 6-hydroxyl groups are nearly equidistant from the ATP gamma-phosphate in catalytically productive phosphoacceptor positions and explains the unusual dual site specificity of this kinase. Inositol tris- and tetrakisphosphates interact via three phosphate binding subsites and one solvent-exposed site that could in principle be occupied by 18 different substrates, explaining the mechanisms for the multiple specificities and catalytic activities of this enzyme.

PubMed: 15837423
DOI: 10.1016/j.molcel.2005.03.016

実験手法

X-RAY DIFFRACTION (1.24 Å)