2abh: Difference between revisions

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[[Image:2abh.~~gif~~|left|200px]]

[[Image:2abh.png|left|200px]]

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~~'''~~PHOSPHATE-BINDING PROTEIN (RE-REFINED)~~'''~~

===PHOSPHATE-BINDING PROTEIN (RE-REFINED)===

~~==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.

The line below this paragraph, {{ABSTRACT_PUBMED_8652549}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 8652549 is the PubMed ID number.

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==About this Structure==

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[[Category: Phosphotransferase]]

[[Category: Transport]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 18~~:50:57 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:59:26 2008''

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-[[Image:2abh.gif|left|200px]]
+{{Seed}}
+[[Image:2abh.png|left|200px]]
 <!--
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 {{STRUCTURE_2abh|  PDB=2abh  |  SCENE=  }}
-'''PHOSPHATE-BINDING PROTEIN (RE-REFINED)'''
+===PHOSPHATE-BINDING PROTEIN (RE-REFINED)===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_8652549}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8652549 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8652549}}
 ==About this Structure==
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 [[Category: Phosphotransferase]]
 [[Category: Transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 18:50:57 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:59:26 2008''