1quj: Difference between revisions

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[[Image:1quj.jpg|left|200px]]
{{Seed}}
[[Image:1quj.png|left|200px]]


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{{STRUCTURE_1quj|  PDB=1quj  |  SCENE=  }}  
{{STRUCTURE_1quj|  PDB=1quj  |  SCENE=  }}  


'''PHOSPHATE-BINDING PROTEIN MUTANT WITH ASP 137 REPLACED BY GLY COMPLEX WITH CHLORINE AND PHOSPHATE'''
===PHOSPHATE-BINDING PROTEIN MUTANT WITH ASP 137 REPLACED BY GLY COMPLEX WITH CHLORINE AND PHOSPHATE===




==Overview==
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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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{{ABSTRACT_PUBMED_8652549}}


==About this Structure==
==About this Structure==
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[[Category: Binding protein]]
[[Category: Binding protein]]
[[Category: Phosphate transport]]
[[Category: Phosphate transport]]
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Revision as of 01:31, 28 July 2008

File:1quj.png

Template:STRUCTURE 1quj

PHOSPHATE-BINDING PROTEIN MUTANT WITH ASP 137 REPLACED BY GLY COMPLEX WITH CHLORINE AND PHOSPHATE

Template:ABSTRACT PUBMED 8652549

About this Structure

1QUJ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Modulation of a salt link does not affect binding of phosphate to its specific active transport receptor., Yao N, Ledvina PS, Choudhary A, Quiocho FA, Biochemistry. 1996 Feb 20;35(7):2079-85. PMID:8652549

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