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[[Image:1k4c.gif|left|200px]]


{{Structure
==Potassium Channel KcsA-Fab complex in high concentration of K+==
|PDB= 1k4c |SIZE=350|CAPTION= <scene name='initialview01'>1k4c</scene>, resolution 2.00&Aring;
<StructureSection load='1k4c' size='340' side='right'caption='[[1k4c]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=DGA:DIACYL+GLYCEROL'>DGA</scene>, <scene name='pdbligand=F09:NONAN-1-OL'>F09</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>
<table><tr><td colspan='2'>[[1k4c]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. The February 2003 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Potassium Channels''  by Shuchismita Dutta and David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2003_2 10.2210/rcsb_pdb/mom_2003_2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K4C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K4C FirstGlance]. <br>
|ACTIVITY=  
</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&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DGA:DIACYL+GLYCEROL'>DGA</scene>, <scene name='pdbligand=F09:NONAN-1-OL'>F09</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k4c OCA], [https://pdbe.org/1k4c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k4c RCSB], [https://www.ebi.ac.uk/pdbsum/1k4c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k4c ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k4c OCA], [http://www.ebi.ac.uk/pdbsum/1k4c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k4c RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/KCSA_STRLI KCSA_STRLI] Acts as a pH-gated potassium ion channel; changing the cytosolic pH from 7 to 4 opens the channel, although it is not clear if this is the physiological stimulus for channel opening. Monovalent cation preference is K(+) > Rb(+) > NH4(+) >> Na(+) > Li(+).<ref>PMID:7489706</ref>
== 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/k4/1k4c_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1k4c ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ion transport proteins must remove an ion's hydration shell to coordinate the ion selectively on the basis of its size and charge. To discover how the K+ channel solves this fundamental aspect of ion conduction, we solved the structure of the KcsA K+ channel in complex with a monoclonal Fab antibody fragment at 2.0 A resolution. Here we show how the K+ channel displaces water molecules around an ion at its extracellular entryway, and how it holds a K+ ion in a square antiprism of water molecules in a cavity near its intracellular entryway. Carbonyl oxygen atoms within the selectivity filter form a very similar square antiprism around each K+ binding site, as if to mimic the waters of hydration. The selectivity filter changes its ion coordination structure in low K+ solutions. This structural change is crucial to the operation of the selectivity filter in the cellular context, where the K+ ion concentration near the selectivity filter varies in response to channel gating.


'''Potassium Channel KcsA-Fab complex in high concentration of K+'''
Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution.,Zhou Y, Morais-Cabral JH, Kaufman A, MacKinnon R Nature. 2001 Nov 1;414(6859):43-8. PMID:11689936<ref>PMID:11689936</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1k4c" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
Ion transport proteins must remove an ion's hydration shell to coordinate the ion selectively on the basis of its size and charge. To discover how the K+ channel solves this fundamental aspect of ion conduction, we solved the structure of the KcsA K+ channel in complex with a monoclonal Fab antibody fragment at 2.0 A resolution. Here we show how the K+ channel displaces water molecules around an ion at its extracellular entryway, and how it holds a K+ ion in a square antiprism of water molecules in a cavity near its intracellular entryway. Carbonyl oxygen atoms within the selectivity filter form a very similar square antiprism around each K+ binding site, as if to mimic the waters of hydration. The selectivity filter changes its ion coordination structure in low K+ solutions. This structural change is crucial to the operation of the selectivity filter in the cellular context, where the K+ ion concentration near the selectivity filter varies in response to channel gating.
*[[Antibody 3D structures|Antibody 3D structures]]
 
*[[Potassium Channel|Potassium Channel]]
==About this Structure==
*[[Potassium channel 3D structures|Potassium channel 3D structures]]
1K4C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. The following page contains interesting information on the relation of 1K4C with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb38_1.html Potassium Channels]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K4C OCA].
*[[3D structures of non-human antibody|3D structures of non-human antibody]]
 
== References ==
==Reference==
<references/>
Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution., Zhou Y, Morais-Cabral JH, Kaufman A, MacKinnon R, Nature. 2001 Nov 1;414(6859):43-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11689936 11689936]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Potassium Channels]]
[[Category: Potassium Channels]]
[[Category: Single protein]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Streptomyces lividans]]
[[Category: Streptomyces lividans]]
[[Category: Kaufman, A.]]
[[Category: Kaufman A]]
[[Category: MacKinnon, R.]]
[[Category: MacKinnon R]]
[[Category: Morais-Cabral, J H.]]
[[Category: Morais-Cabral JH]]
[[Category: Zhou, Y.]]
[[Category: Zhou Y]]
[[Category: k channel]]
[[Category: protein-antibody fab complex]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:43:13 2008''
Retrieved from "https://proteopedia.org/1k4c"