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PDBsum entry 1frp
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Hydrolase(phosphoric monoester)
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PDB id
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1frp
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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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Crystal structure of fructose-1,6-Bisphosphatase complexed with fructose 2,6-Bisphosphate, Amp, And zn2+ at 2.0-A resolution: aspects of synergism between inhibitors.
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Authors
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Y.Xue,
S.Huang,
J.Y.Liang,
Y.Zhang,
W.N.Lipscomb.
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Ref.
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Proc Natl Acad Sci U S A, 1994,
91,
12482-12486.
[DOI no: ]
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PubMed id
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Abstract
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The crystal structure of fructose-1,6-bisphosphatase (Fru-1,6-Pase; EC 3.1.3.11)
complexed with Zn2+ and two allosteric regulators, AMP and fructose
2,6-bisphosphate (Fru-2,6-P2) has been determined at 2.0-A resolution. In the
refined model, the crystallographic R factor is 0.189 with rms deviations of
0.014 A and 2.8 degrees from ideal geometries for bond lengths and bond angles,
respectively. A 15 degrees rotation is observed between the upper dimer C1C2 and
the lower dimer C3C4 relative to the R-form structure (fructose 6-phosphate
complex), consistent with that expected from a T-form structure. The major
difference between the structure of the previously determined Fru-2,6-P2 complex
(R form) and that of the current quaternary T-form complex lies in the active
site domain. A zinc binding site distinct from the three binding sites
established earlier was identified within each monomer. Helix H4 (residues
123-127) was found to be better defined than in previously studied ligated
Fru-1,6-Pase structures. Interactions between monomers in the active site domain
were found involving H4 residues from one monomer and residues Tyr-258 and
Arg-243 from the adjacent monomer. Cooperativity between AMP and Fru-2,6-P2 in
signal transmission probably involves the following features: an AMP site, the
adjacent B3 strand (residues 113-118), the metal site, the immediate active
site, the short helix H4 (residues 123-127), and Tyr-258 and Arg-243 from the
adjacent monomer within the upper (or lower) dimer. The closest distance between
the immediate active site and that on the adjacent monomer is only 5 A. Thus,
the involvement of H4 in signal transmission adds another important pathway to
the scheme of the allosteric mechanism of Fru-1,6-Pase.
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Secondary reference #1
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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 #2
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Title
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Crystal structure of the neutral form of fructose 1,6-Bisphosphatase complexed with regulatory inhibitor fructose 2,6-Bisphosphate at 2.6-A resolution.
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Authors
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J.Y.Liang,
S.Huang,
Y.Zhang,
H.Ke,
W.N.Lipscomb.
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Ref.
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Proc Natl Acad Sci U S A, 1992,
89,
2404-2408.
[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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