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New page: left|200px<br /><applet load="2h8p" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h8p, resolution 2.25Å" /> '''Structure of a K cha...
 
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[[Image:2h8p.jpg|left|200px]]<br /><applet load="2h8p" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2h8p, resolution 2.25&Aring;" />
'''Structure of a K channel with an amide to ester substitution in the selectivity filter'''<br />


==Overview==
==Structure of a K channel with an amide to ester substitution in the selectivity filter==
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.
<StructureSection load='2h8p' size='340' side='right'caption='[[2h8p]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2h8p]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H8P 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]] 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=K:POTASSIUM+ION'>K</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=2h8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h8p OCA], [https://pdbe.org/2h8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h8p RCSB], [https://www.ebi.ac.uk/pdbsum/2h8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h8p 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/h8/2h8p_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=2h8p ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2H8P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with K, GOA and B3H as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2H8P OCA].
*[[Antibody 3D structures|Antibody 3D structures]]
 
*[[Potassium channel 3D structures|Potassium channel 3D structures]]
==Reference==
*[[3D structures of non-human antibody|3D structures of non-human antibody]]
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16939283 16939283]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Streptomyces lividans]]
[[Category: MacKinnon, R.]]
[[Category: MacKinnon R]]
[[Category: Muir, T.W.]]
[[Category: Muir TW]]
[[Category: Valiyaveetil, F.I.]]
[[Category: Valiyaveetil FI]]
[[Category: B3H]]
[[Category: GOA]]
[[Category: K]]
[[Category: channel]]
[[Category: ester]]
[[Category: semi-synthetic]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:36:29 2007''

Latest revision as of 10:15, 27 March 2024

Structure of a K channel with an amide to ester substitution in the selectivity filter

2h8p, resolution 2.25Å

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