2hfe: Difference between revisions

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-[[Image:2hfe.jpg|left|200px]]
-<!--
+==Rb+ complex of a K channel with an amide to ester substitution in the selectivity filter==
-The line below this paragraph, containing "STRUCTURE_2hfe", creates the "Structure Box" on the page.
+<StructureSection load='2hfe' size='340' side='right'caption='[[2hfe]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2hfe]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Streptomyces_coelicolor_A3(2) Streptomyces coelicolor A3(2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HFE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HFE FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B3H:(2S)-2-(BUTYRYLOXY)-3-HYDROXYPROPYL+NONANOATE'>B3H</scene>, <scene name='pdbligand=GOA:GLYCOLIC+ACID'>GOA</scene>, <scene name='pdbligand=RB:RUBIDIUM+ION'>RB</scene></td></tr>
-{{STRUCTURE_2hfe|  PDB=2hfe  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hfe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hfe OCA], [https://pdbe.org/2hfe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hfe RCSB], [https://www.ebi.ac.uk/pdbsum/2hfe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hfe ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q569B4_RAT Q569B4_RAT]
+== 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/hf/2hfe_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=2hfe ConSurf].
+<div style="clear:both"></div>
-'''Rb+ complex of a K channel with an amide to ester substitution in the selectivity filter'''
+==See Also==
+*[[Antibody 3D structures|Antibody 3D structures]]
+*[[Potassium channel 3D structures|Potassium channel 3D structures]]
-==Overview==
+*[[3D structures of non-human antibody|3D structures of non-human antibody]]
-The selectivity filter of K(+) channels comprises four contiguous ion binding sites, S1 through S4. Structural and functional data indicate that the filter contains on average two K(+) ions at any given time and that these ions reside primarily in two configurations, namely to sites S1 and S3 or to sites S2 and S4. Maximum ion flux through the channel is expected to occur when the energy difference between these two binding configurations is zero. In this study, we have used protein semisynthesis to selectively perturb site 1 within the filter of the KcsA channel through use of an amide-to-ester substitution. The modification alters K(+) conduction properties. The structure of the selectivity filter is largely unperturbed by the modification, despite the loss of an ordered water molecule normally located just behind the filter. Introduction of the ester moiety was found to alter the distribution of K(+), Rb(+,) and Cs(+) within the filter, with the most dramatic change found for Rb(+). The redistribution of ions is associated with the appearance of a partially hydrated ion just external to the filter, at a position where no ion is observed in the wild-type channel. The appearance of this new ion-binding site creates a change in the distance between a pair of K(+) ions some fraction of the time, apparently leading to a reduction in the ion conduction rate. Importantly, this finding suggests that the selectivity filter of a potassium channel is optimized both in terms of absolute ion occupancy and in terms of the separation in distance between the conducting ions.
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-HFE is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HFE OCA].
-==Reference==
-Structural and functional consequences of an amide-to-ester substitution in the selectivity filter of a potassium channel., Valiyaveetil FI, Sekedat M, MacKinnon R, Muir TW, J Am Chem Soc. 2006 Sep 6;128(35):11591-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16939283 16939283]
 [[Category: Mus musculus]]
-[[Category: Protein complex]]
+[[Category: MacKinnon R]]
-[[Category: MacKinnon, R.]]
+[[Category: Muir TW]]
-[[Category: Muir, T W.]]
+[[Category: Valiyaveetil FI]]
-[[Category: Valiyaveetil, F I.]]
-[[Category: Channel]]
-[[Category: Ester]]
-[[Category: Semi-synthetic]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 06:13:40 2008''