2abh

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{{STRUCTURE_2abh| PDB=2abh | SCENE= }}
{{STRUCTURE_2abh| PDB=2abh | SCENE= }}
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'''PHOSPHATE-BINDING PROTEIN (RE-REFINED)'''
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===PHOSPHATE-BINDING PROTEIN (RE-REFINED)===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 8652549 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8652549}}
==About this Structure==
==About this Structure==
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[[Category: Phosphotransferase]]
[[Category: Phosphotransferase]]
[[Category: Transport]]
[[Category: Transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:59:26 2008''

Revision as of 01:59, 29 July 2008

Image:2abh.png

Template:STRUCTURE 2abh

PHOSPHATE-BINDING PROTEIN (RE-REFINED)

Template:ABSTRACT PUBMED 8652549

About this Structure

2ABH is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1abh. 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

Page seeded by OCA on Tue Jul 29 04:59:26 2008

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