View source for 3beh


==Structure of a Bacterial Cyclic Nucleotide Regulated Ion Channel==
<StructureSection load='3beh' size='340' side='right' caption='[[3beh]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3beh]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_700743 Atcc 700743]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BEH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BEH FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3beh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3beh OCA], [http://pdbe.org/3beh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3beh RCSB], [http://www.ebi.ac.uk/pdbsum/3beh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3beh ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/CNGK1_RHILO CNGK1_RHILO]] Cyclic nucleotide-regulated potassium channel activated by cAMP.<ref>PMID:15550244</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/be/3beh_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=3beh ConSurf].
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== Publication Abstract from PubMed ==
The six-transmembrane helix (6 TM) tetrameric cation channels form the largest ion channel family, some members of which are voltage-gated and others are not. There are no reported channel structures to match the wealth of functional data on the non-voltage-gated members. We determined the structure of the transmembrane regions of the bacterial cyclic nucleotide-regulated channel MlotiK1, a non-voltage-gated 6 TM channel. The structure showed how the S1-S4 domain and its associated linker can serve as a clamp to constrain the gate of the pore and possibly function in concert with ligand-binding domains to regulate the opening of the pore. The structure also led us to hypothesize a new mechanism by which motions of the S6 inner helices can gate the ion conduction pathway at a position along the pore closer to the selectivity filter than the canonical helix bundle crossing.

Structure of the transmembrane regions of a bacterial cyclic nucleotide-regulated channel.,Clayton GM, Altieri S, Heginbotham L, Unger VM, Morais-Cabral JH Proc Natl Acad Sci U S A. 2008 Feb 5;105(5):1511-5. Epub 2008 Jan 23. PMID:18216238<ref>PMID:18216238</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3beh" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ion channels|Ion channels]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Atcc 700743]]
[[Category: Clayton, G M]]
[[Category: Morais-Cabral, J H]]
[[Category: Membrane protein]]
[[Category: Transmembrane protein]]