1i9y
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(New page: 200px<br /><applet load="1i9y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i9y, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 15:05, 20 November 2007
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CRYSTAL STRUCTURE OF INOSITOL POLYPHOSPHATE 5-PHOSPHATASE DOMAIN (IPP5C) OF SPSYNAPTOJANIN
Overview
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.
About this Structure
1I9Y is a Single protein structure of sequence from Schizosaccharomyces pombe. Full crystallographic information is available from OCA.
Reference
Specificity determinants in phosphoinositide dephosphorylation: crystal structure of an archetypal inositol polyphosphate 5-phosphatase., Tsujishita Y, Guo S, Stolz LE, York JD, Hurley JH, Cell. 2001 May 4;105(3):379-89. PMID:11348594
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