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PDBsum entry 1djx
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Lipid degradation
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PDB id
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1djx
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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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Structural mapping of the catalytic mechanism for a mammalian phosphoinositide-Specific phospholipase c.
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Authors
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L.O.Essen,
O.Perisic,
M.Katan,
Y.Wu,
M.F.Roberts,
R.L.Williams.
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Ref.
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Biochemistry, 1997,
36,
1704-1718.
[DOI no: ]
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PubMed id
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Abstract
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The crystal structures of various ternary complexes of phosphoinositide-specific
phospholipase C-delta 1 from rat with calcium and inositol phosphates have been
determined at 2.30-2.95 A resolution. The inositol phosphates used in this study
mimic the binding of substrates and the reaction intermediate and include
D-myo-inositol-1,4,5-trisphosphate, D-myo-inositol-2,4, 5-trisphosphate.
D-myo-inositol-4,5-bisphosphate, and
D,1-myo-inositol-2-methylene-1,2-cyclićmonophosphonate. The complexes exhibit
an almost invariant mode of binding in the active site, each fitting edge-on
into the active site and interacting with both the enzyme and the catalytic
calcium at the bottom of the active site. Most of the active site residues do
not undergo conformational changes upon binding either calcium or inositol
phosphates. The structures are consistent with bidentate liganding of the
catalytic calcium to the inositol phosphate intermediate and transition state.
The complexes suggest explanations for substrate preference, pH optima, and
ratio of cyclic to acyclic reaction products. A reaction mechanism is derived
that supports general acid/base catalysis in a sequential mechanism involving a
cyclic phosphate intermediate and rules out a parallel mechanism where acyclic
and cyclic products are simultaneously generated.
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Secondary reference #1
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Title
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Crystal structure of a mammalian phosphoinositide-Specific phospholipase c delta.
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Authors
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L.O.Essen,
O.Perisic,
R.Cheung,
M.Katan,
R.L.Williams.
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Ref.
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Nature, 1996,
380,
595-602.
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PubMed id
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