1I9Y

CRYSTAL STRUCTURE OF INOSITOL POLYPHOSPHATE 5-PHOSPHATASE DOMAIN (IPP5C) OF SPSYNAPTOJANIN

Summary for 1I9Y

• Entry DOI: 10.2210/pdb1i9y/pdb
• Related: 1I9Z
• Descriptor: PHOSPHATIDYLINOSITOL PHOSPHATE PHOSPHATASE (2 entities in total)
• Functional Keywords: ipp5c, inositol 5-phosphatase, hydrolase
• Biological source: Schizosaccharomyces pombe (fission yeast)
• Total number of polymer chains: 1
• Total formula weight: 40094.21

Authors

Tsujishita, Y.,Guo, S.,Stolz, L.,York, J.D.,Hurley, J.H. (deposition date: 2001-03-21, release date: 2001-05-16, Last modification date: 2024-02-07)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2 Å)