1qul: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1qul.jpg|left|200px]]<br /><applet load="1qul" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1qul, resolution 1.7&Aring;" />
-'''PHOSPHATE-BINDING PROTEIN MUTANT WITH ASP 137 REPLACED BY THR COMPLEX WITH CHLORINE AND PHOSPHATE'''<br />
-==Overview==
+==PHOSPHATE-BINDING PROTEIN MUTANT WITH ASP 137 REPLACED BY THR COMPLEX WITH CHLORINE AND PHOSPHATE==
-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.
+<StructureSection load='1qul' size='340' side='right'caption='[[1qul]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1qul]] 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=1QUL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QUL FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qul OCA], [https://pdbe.org/1qul PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qul RCSB], [https://www.ebi.ac.uk/pdbsum/1qul PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qul ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PSTS_ECOLI PSTS_ECOLI] Part of the ABC transporter complex PstSACB involved in phosphate import.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qu/1qul_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1qul ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-QUL 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 PO4 and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QUL OCA].
+*[[Phosphate-binding protein|Phosphate-binding protein]]
+__TOC__
-==Reference==
+</StructureSection>
-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]
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Choudhary, A.]]
+[[Category: Choudhary A]]
-[[Category: Ledvina, P.S.]]
+[[Category: Ledvina PS]]
-[[Category: Quiocho, F.A.]]
+[[Category: Quiocho FA]]
-[[Category: Yao, N.]]
+[[Category: Yao N]]
-[[Category: CL]]
-[[Category: PO4]]
-[[Category: binding protein]]
-[[Category: phosphate transport]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:00:10 2007''