2zd9: Difference between revisions
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==Structure of a Bacterial Cyclic-Nucleotide Regulated Ion Channel== | ==Structure of a Bacterial Cyclic-Nucleotide Regulated Ion Channel== | ||
<StructureSection load='2zd9' size='340' side='right' caption='[[2zd9]], [[Resolution|resolution]] 4.00Å' scene=''> | <StructureSection load='2zd9' size='340' side='right'caption='[[2zd9]], [[Resolution|resolution]] 4.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2zd9]] 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=2ZD9 OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[2zd9]] 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=2ZD9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2ZD9 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></td></tr> | </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></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3beh|3beh]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3beh|3beh]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2zd9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zd9 OCA], [http://pdbe.org/2zd9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zd9 RCSB], [http://www.ebi.ac.uk/pdbsum/2zd9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zd9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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==See Also== | ==See Also== | ||
*[[Ion channels|Ion channels]] | *[[Ion channels 3D structures|Ion channels 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Atcc 700743]] | [[Category: Atcc 700743]] | ||
[[Category: Large Structures]] | |||
[[Category: Cabral-Morais, J M]] | [[Category: Cabral-Morais, J M]] | ||
[[Category: Clayton, G M]] | [[Category: Clayton, G M]] | ||
[[Category: Membrane protein]] | [[Category: Membrane protein]] | ||
[[Category: Transmembrane protein]] | [[Category: Transmembrane protein]] | ||
Revision as of 15:02, 29 July 2020
Structure of a Bacterial Cyclic-Nucleotide Regulated Ion ChannelStructure of a Bacterial Cyclic-Nucleotide Regulated Ion Channel
Structural highlights
Function[CNGK1_RHILO] Cyclic nucleotide-regulated potassium channel activated by cAMP.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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