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 2.0&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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'''CRYSTAL STRUCTURE OF INOSITOL POLYPHOSPHATE 5-PHOSPHATASE DOMAIN (IPP5C) OF SPSYNAPTOJANIN'''<br />
'''CRYSTAL STRUCTURE OF INOSITOL POLYPHOSPHATE 5-PHOSPHATASE DOMAIN (IPP5C) OF SPSYNAPTOJANIN'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1I9Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I9Y OCA].
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1I9Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I9Y OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Guo, S.]]
[[Category: Guo, S.]]
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[[Category: Hurley, J.H.]]
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[[Category: Hurley, J H.]]
[[Category: Stolz, L.]]
[[Category: Stolz, L.]]
[[Category: Tsujishita, Y.]]
[[Category: Tsujishita, Y.]]
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[[Category: York, J.D.]]
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[[Category: York, J D.]]
[[Category: inositol 5-phosphatase]]
[[Category: inositol 5-phosphatase]]
[[Category: ipp5c]]
[[Category: ipp5c]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:12:14 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:09:38 2008''

Revision as of 11:09, 21 February 2008


1i9y, resolution 2.0Å

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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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