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PDBsum entry 1quj
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Phosphate transport
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PDB id
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1quj
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References listed in PDB file
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Key reference
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Title
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Modulation of a salt link does not affect binding of phosphate to its specific active transport receptor.
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Authors
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N.Yao,
P.S.Ledvina,
A.Choudhary,
F.A.Quiocho.
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Ref.
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Biochemistry, 1996,
35,
2079-2085.
[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
perfect match.
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Abstract
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Electrostatic interactions are among the key forces determining the structure
and function of proteins. These are exemplified in the liganded form of the
receptor, a phosphate binding protein from Escherichia coli. The phosphate,
completely dehydrated and buried in the receptor, is bound by 12 hydrogen bonds
as well as a salt link with Arg 135. We have modulated the ionic attraction
while preserving the hydrogen bonds by mutating Asp 137, also salt linked to Arg
135, to Asn, Gly or Thr. High-resolution crystallographic analysis revealed that
Gly and Thr (but not Asn) mutant proteins have incorporated a more
electronegative Cl- in place of the Asp carboxylate. That no dramatic effect on
phosphate affinity was produced by these ionic perturbations indicates a major
role for hydrogen bonds and other local dipoles in the binding and charge
stabilization of ionic ligands.
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Secondary reference #1
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Title
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Fine tuning the specificity of the periplasmic phosphate transport receptor. Site-Directed mutagenesis, Ligand binding, And crystallographic studies.
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Authors
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Z.Wang,
A.Choudhary,
P.S.Ledvina,
F.A.Quiocho.
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Ref.
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J Biol Chem, 1994,
269,
25091-25094.
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PubMed id
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Secondary reference #2
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Title
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High specificity of a phosphate transport protein determined by hydrogen bonds.
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Authors
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H.Luecke,
F.A.Quiocho.
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Ref.
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Nature, 1990,
347,
402-406.
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PubMed id
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