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1qui

From Proteopedia

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[[Image:1qui.jpg|left|200px]]<br /><applet load="1qui" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1qui, resolution 1.9&Aring;" />
 
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'''PHOSPHATE-BINDING PROTEIN MUTANT WITH ASP 137 REPLACED BY GLY COMPLEX WITH BROMINE AND PHOSPHATE'''<br />
 
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==Overview==
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==PHOSPHATE-BINDING PROTEIN MUTANT WITH ASP 137 REPLACED BY GLY COMPLEX WITH BROMINE AND PHOSPHATE==
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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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<StructureSection load='1qui' size='340' side='right'caption='[[1qui]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1qui]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QUI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QUI FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qui OCA], [https://pdbe.org/1qui PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qui RCSB], [https://www.ebi.ac.uk/pdbsum/1qui PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qui ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PSTS_ECOLI PSTS_ECOLI] Part of the ABC transporter complex PstSACB involved in phosphate import.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qu/1qui_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qui ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1QUI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=BR:'>BR</scene> and <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QUI OCA].
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*[[Phosphate-binding protein|Phosphate-binding protein]]
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__TOC__
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==Reference==
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</StructureSection>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=8652549 8652549]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Choudhary, A.]]
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[[Category: Choudhary A]]
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[[Category: Ledvina, P S.]]
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[[Category: Ledvina PS]]
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[[Category: Quiocho, F A.]]
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[[Category: Quiocho FA]]
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[[Category: Yao, N.]]
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[[Category: Yao N]]
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[[Category: BR]]
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[[Category: PO4]]
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[[Category: binding protein]]
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[[Category: phosphate transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:43:55 2008''
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Current revision

PHOSPHATE-BINDING PROTEIN MUTANT WITH ASP 137 REPLACED BY GLY COMPLEX WITH BROMINE AND PHOSPHATE

PDB ID 1qui

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