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3k0d

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<StructureSection load='3k0d' size='340' side='right'caption='[[3k0d]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
<StructureSection load='3k0d' size='340' side='right'caption='[[3k0d]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3k0d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14579 Atcc 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K0D OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3K0D FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3k0d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K0D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K0D FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3k03|3k03]], [[3k04|3k04]], [[3k06|3k06]], [[3k08|3k08]], [[3k0g|3k0g]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3k0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k0d OCA], [http://pdbe.org/3k0d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3k0d RCSB], [http://www.ebi.ac.uk/pdbsum/3k0d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3k0d ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3k0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k0d OCA], [https://pdbe.org/3k0d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k0d RCSB], [https://www.ebi.ac.uk/pdbsum/3k0d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k0d ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q81HW2_BACCR Q81HW2_BACCR]
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Cyclic nucleotide-gated (CNG) channels play an essential role in the visual and olfactory sensory systems and are ubiquitous in eukaryotes. Details of their underlying ion selectivity properties are still not fully understood and are a matter of debate in the absence of high-resolution structures. To reveal the structural mechanism of ion selectivity in CNG channels, particularly their Ca(2+) blockage property, we engineered a set of mimics of CNG channel pores for both structural and functional analysis. The mimics faithfully represent the CNG channels they are modeled after, permeate Na(+) and K(+) equally well, and exhibit the same Ca(2+) blockage and permeation properties. Their high-resolution structures reveal a hitherto unseen selectivity filter architecture comprising three contiguous ion binding sites in which Na(+) and K(+) bind with different ion-ligand geometries. Our structural analysis reveals that the conserved acidic residue in the filter is essential for Ca(2+) binding but not through direct ion chelation as in the currently accepted view. Furthermore, structural insight from our CNG mimics allows us to pinpoint equivalent interactions in CNG channels through structure-based mutagenesis that have previously not been predicted using NaK or K(+) channel models.
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Structural studies of ion permeation and Ca2+ blockage of a bacterial channel mimicking the cyclic nucleotide-gated channel pore.,Derebe MG, Zeng W, Li Y, Alam A, Jiang Y Proc Natl Acad Sci U S A. 2010 Dec 27. PMID:21187429<ref>PMID:21187429</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3k0d" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Potassium channel 3D structures|Potassium channel 3D structures]]
*[[Potassium channel 3D structures|Potassium channel 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 14579]]
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[[Category: Bacillus cereus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Derebe, M G]]
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[[Category: Derebe MG]]
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[[Category: Jiang, Y]]
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[[Category: Jiang Y]]
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[[Category: Cng channel selectivity filter]]
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[[Category: Cng mimicking]]
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[[Category: Etpp]]
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[[Category: Ionic channel]]
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[[Category: Nak]]
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[[Category: Nak-etpp]]
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[[Category: Nak-mutant]]
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[[Category: Transport protein]]
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Current revision

Crystal Structure of CNG mimicking NaK mutant, NaK-ETPP, K+ complex

PDB ID 3k0d

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