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PDBsum entry 1i9z
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Specificity determinants in phosphoinositide dephosphorylation: crystal structure of an archetypal inositol polyphosphate 5-Phosphatase.
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Authors
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Y.Tsujishita,
S.Guo,
L.E.Stolz,
J.D.York,
J.H.Hurley.
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Ref.
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Cell, 2001,
105,
379-389.
[DOI no: ]
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PubMed id
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Abstract
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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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Figure 1.
Figure 1. Domain Structures of Representa-
tive 5-Phosphatases
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Figure 7.
Figure 7. Membrane Docking of SPsynapto-
janin-IPP5C
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The above figures are
reprinted
by permission from Cell Press:
Cell
(2001,
105,
379-389)
copyright 2001.
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