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PDBsum entry 1ptg
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Hydrolase (phosphoric diester)
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PDB id
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1ptg
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the phosphatidylinositol-Specific phospholipase c from bacillus cereus in complex with myo-Inositol.
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Authors
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D.W.Heinz,
M.Ryan,
T.L.Bullock,
O.H.Griffith.
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Ref.
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Embo J, 1995,
14,
3855-3863.
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PubMed id
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Abstract
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Phosphatidylinositol (PI), once regarded as an obscure component of membranes,
is now recognized as an important reservoir of second messenger precursors and
as an anchor for membrane enzymes. PI-specific phospholipase C (PI-PLC) is the
enzyme that cleaves PI, invoking numerous cellular responses. The crystal
structure of PI-PLC from Bacillus cereus (EC 3.1.4.10) has been solved at 2.6 A
resolution and refined to a crystallographic R factor of 18.7%. The structure
consists of an imperfect (beta alpha)8-barrel similar to that first observed for
triose phosphate isomerase and does not resemble any other known phospholipase
structure. The active site of the enzyme has been identified by determining the
structure of PI-PLC in complex with its inhibitor, myo-inositol, at 2.6 A
resolution (R factor = 19.5%). This substrate-like inhibitor interacts with a
number of residues highly conserved among prokaryotic PI-PLCs. Residues His32
and His82, which are also conserved between prokaryotic and eukaryotic PI-PLCs,
most likely act as general base and acid respectively in a catalytic mechanism
analogous to that observed for ribonucleases.
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Secondary reference #1
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Title
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Crystallization of phosphatidylinositol-Specific phospholipase c from bacillus cereus.
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Authors
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T.L.Bullock,
M.Ryan,
S.L.Kim,
S.J.Remington,
O.H.Griffith.
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Ref.
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Biophys J, 1993,
64,
784-791.
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PubMed id
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Secondary reference #2
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Title
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Phosphatidylinositol-Specific phospholipase c of bacillus cereus: cloning, Sequencing, And relationship to other phospholipases.
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Authors
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A.Kuppe,
L.M.Evans,
D.A.Mcmillen,
O.H.Griffith.
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Ref.
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J Bacteriol, 1989,
171,
6077-6083.
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PubMed id
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