1I9Z

CRYSTAL STRUCTURE OF INOSITOL POLYPHOSPHATE 5-PHOSPHATASE DOMAIN (IPP5C) OF SPSYNAPTOJANIN IN COMPLEX WITH INOSITOL (1,4)-BISPHOSPHATE AND CALCIUM ION

1I9Z の概要

• エントリーDOI: 10.2210/pdb1i9z/pdb
• 関連するPDBエントリー: 1I9Y
• 分子名称: PHOSPHATIDYLINOSITOL PHOSPHATE PHOSPHATASE, CALCIUM ION, D-MYO-INOSITOL-1,4-BISPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: spsynaptojanin, ipp5c, ip3, ip2, hydrolase
• 由来する生物種: Schizosaccharomyces pombe (fission yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40474.41

構造登録者

Tsujishita, Y.,Guo, S.,Stolz, L.,York, J.D.,Hurley, J.H. (登録日: 2001-03-21, 公開日: 2001-05-16, 最終更新日: 2024-02-07)

主引用文献

Tsujishita, Y.,Guo, S.,Stolz, L.E.,York, J.D.,Hurley, J.H.
Specificity determinants in phosphoinositide dephosphorylation: crystal structure of an archetypal inositol polyphosphate 5-phosphatase.
Cell(Cambridge,Mass.), 105:379-389, 2001

PubMed Abstract: Inositol polyphosphate 5-phosphatases are central to intracellular processes ranging from membrane trafficking to Ca(2+) signaling, and defects in this activity result in the human disease Lowe syndrome. The 1.8 resolution structure of the inositol polyphosphate 5-phosphatase domain of SPsynaptojanin bound to Ca(2+) and inositol (1,4)-bisphosphate reveals a fold and an active site His and Asp pair resembling those of several Mg(2+)-dependent nucleases. Additional loops mediate specific inositol polyphosphate contacts. The 4-phosphate of inositol (1,4)-bisphosphate is misoriented by 4.6 compared to the reactive geometry observed in the apurinic/apyrimidinic endonuclease 1, explaining the dephosphorylation site selectivity of the 5-phosphatases. Based on the structure, a series of mutants are described that exhibit altered substrate specificity providing general determinants for substrate recognition.

PubMed: 11348594
DOI: 10.1016/S0092-8674(01)00326-9

実験手法

X-RAY DIFFRACTION (1.8 Å)