1oib
From Proteopedia
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| - | [[Image:1oib.gif|left|200px]] | + | [[Image:1oib.gif|left|200px]] |
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| - | '''PHOSPHATE-BINDING PROTEIN MUTANT T141D''' | + | {{Structure |
| + | |PDB= 1oib |SIZE=350|CAPTION= <scene name='initialview01'>1oib</scene>, resolution 2.4Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= PHOS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''PHOSPHATE-BINDING PROTEIN MUTANT T141D''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OIB is a [ | + | 1OIB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OIB OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8652549 8652549] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: phosphate transport]] | [[Category: phosphate transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:11:16 2008'' |
Revision as of 11:11, 20 March 2008
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| , resolution 2.4Å | |||||||
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| Gene: | PHOS (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PHOSPHATE-BINDING PROTEIN MUTANT T141D
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.
About this Structure
1OIB 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
Page seeded by OCA on Thu Mar 20 13:11:16 2008
