1oib: Difference between revisions

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[[Image:1oib.gif|left|200px]]
[[Image:1oib.gif|left|200px]]


{{Structure
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|GENE= PHOS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oib OCA], [http://www.ebi.ac.uk/pdbsum/1oib PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oib RCSB]</span>
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'''PHOSPHATE-BINDING PROTEIN MUTANT T141D'''
'''PHOSPHATE-BINDING PROTEIN MUTANT T141D'''
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[[Category: Quiocho, F A.]]
[[Category: Quiocho, F A.]]
[[Category: Yao, N.]]
[[Category: Yao, N.]]
[[Category: phosphate transport]]
[[Category: Phosphate transport]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:45:47 2008''

Revision as of 03:53, 3 May 2008

File:1oib.gif

Template:STRUCTURE 1oib

PHOSPHATE-BINDING PROTEIN MUTANT T141D


OverviewOverview

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.

About this StructureAbout this Structure

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

ReferenceReference

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 Sat May 3 03:53:00 2008

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