1qul: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1qul]] is a 1 chain structure with 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=1QUL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QUL FirstGlance]. <br> | <table><tr><td colspan='2'>[[1qul]] is a 1 chain structure with 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=1QUL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QUL FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qul OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qul RCSB], [http://www.ebi.ac.uk/pdbsum/1qul PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qul OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qul RCSB], [http://www.ebi.ac.uk/pdbsum/1qul PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/PSTS_ECOLI PSTS_ECOLI]] Part of the ABC transporter complex PstSACB involved in phosphate import. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 32: | Line 34: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Choudhary, A | [[Category: Choudhary, A]] | ||
[[Category: Ledvina, P S | [[Category: Ledvina, P S]] | ||
[[Category: Quiocho, F A | [[Category: Quiocho, F A]] | ||
[[Category: Yao, N | [[Category: Yao, N]] | ||
[[Category: Binding protein]] | [[Category: Binding protein]] | ||
[[Category: Phosphate transport]] | [[Category: Phosphate transport]] | ||
Revision as of 10:23, 25 December 2014
PHOSPHATE-BINDING PROTEIN MUTANT WITH ASP 137 REPLACED BY THR COMPLEX WITH CHLORINE AND PHOSPHATEPHOSPHATE-BINDING PROTEIN MUTANT WITH ASP 137 REPLACED BY THR COMPLEX WITH CHLORINE AND PHOSPHATE
Structural highlights
Function[PSTS_ECOLI] Part of the ABC transporter complex PstSACB involved in phosphate import. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedElectrostatic 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||