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PDBsum entry 1fpg
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Hydrolase (phosphoric monoester)
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PDB id
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1fpg
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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 aspects of the allosteric inhibition of fructose-1,6-Bisphosphatase by AMP: the binding of both the substrate analogue 2,5-Anhydro-D-Glucitol 1,6-Bisphosphate and catalytic metal ions monitored by X-Ray crystallography.
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Authors
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V.Villeret,
S.Huang,
Y.Zhang,
W.N.Lipscomb.
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Ref.
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Biochemistry, 1995,
34,
4307-4315.
[DOI no: ]
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
94%.
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Abstract
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The crystal structures of the T form pig kidney fructose-1,6-bisphosphatase (EC
3.1.3.11) complexed with AMP, the substrate analogue 2,5-anhydro-D-glucitol
1,6-bisphosphate (AhG-1,6-P2), and Mn2+ at concentrations of 5, 15, 100, and 300
microM have been determined and refined at resolutions of 2.1-2.3 A to R factors
which range from 0.180 to 0.195, respectively. Two metal ions per active site
have been identified, one at a binding site of high affinity (metal site 1'),
the second in a low affinity site (metal site 2'). The 1-phosphate group of the
substrate analogue coordinates to the metal ion at site 1', but not at site 2'.
In these four complexes, the distances between the two metal ions are all within
0.2 A of 4.3 A. In the previously determined R form structure of Fru-1,6-Pase
complexed with AhG-1,6-P2 and Mn2+, there are also two metal ions in the active
site at metal sites 1 and 2. The metal ion at site 1 is only 0.6 A displaced
from the metal ion at site 1' in the T form and is also coordinated to the
1-phosphate group of AhG-1,6-P2. However, the second metal ion is located in two
distinct sites which are 1.4 A apart in the T and R form structures. In the R
form the Mn2+ at site 2 is coordinated to the 1-phosphate group of the substrate
analogue. This metal ion is apparently required to orient the phosphate group
for nucleophilic attack at the phosphorus center.(ABSTRACT TRUNCATED AT 250
WORDS)
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Secondary reference #1
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Title
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Toward a mechanism for the allosteric transition of pig kidney fructose-1,6-Bisphosphatase.
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Authors
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Y.Zhang,
J.Y.Liang,
S.Huang,
W.N.Lipscomb.
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Ref.
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J Mol Biol, 1994,
244,
609-624.
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PubMed id
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Secondary reference #2
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Title
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Crystallographic studies of the catalytic mechanism of the neutral form of fructose-1,6-Bisphosphatase.
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Authors
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Y.Zhang,
J.Y.Liang,
S.Huang,
H.Ke,
W.N.Lipscomb.
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Ref.
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Biochemistry, 1993,
32,
1844-1857.
[DOI no: ]
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PubMed id
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Secondary reference #3
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Title
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Conformational transition of fructose-1,6-Bisphosphatase: structure comparison between the AMP complex (t form) and the fructose 6-Phosphate complex (r form).
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Authors
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H.M.Ke,
J.Y.Liang,
Y.P.Zhang,
W.N.Lipscomb.
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Ref.
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Biochemistry, 1991,
30,
4412-4420.
[DOI no: ]
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PubMed id
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