1zwi
From Proteopedia
(New page: 200px<br /> <applet load="1zwi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zwi, resolution 2.50Å" /> '''Structure of mutant...) |
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| - | [[Image:1zwi.gif|left|200px]]<br /> | + | [[Image:1zwi.gif|left|200px]]<br /><applet load="1zwi" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1zwi" size=" | + | |
caption="1zwi, resolution 2.50Å" /> | caption="1zwi, resolution 2.50Å" /> | ||
'''Structure of mutant KcsA potassium channel'''<br /> | '''Structure of mutant KcsA potassium channel'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We show that in the potassium channel KcsA, proton-dependent activation is | + | We show that in the potassium channel KcsA, proton-dependent activation is followed by an inactivation process similar to C-type inactivation, and this process is suppressed by an E71A mutation in the pore helix. EPR spectroscopy demonstrates that the inner gate opens maximally at low pH regardless of the magnitude of the single-channel-open probability, implying that stationary gating originates mostly from rearrangements at the selectivity filter. Two E71A crystal structures obtained at 2.5 A reveal large structural excursions of the selectivity filter during ion conduction and provide a glimpse of the range of conformations available to this region of the channel during gating. These data establish a mechanistic basis for the role of the selectivity filter during channel activation and inactivation. |
==About this Structure== | ==About this Structure== | ||
| - | 1ZWI is a [http://en.wikipedia.org/wiki/Single_protein 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] with K, DGA and F09 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1ZWI is a [http://en.wikipedia.org/wiki/Single_protein 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] with <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=DGA:'>DGA</scene> and <scene name='pdbligand=F09:'>F09</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZWI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces lividans]] | [[Category: Streptomyces lividans]] | ||
| - | [[Category: Cordero-Morales, J | + | [[Category: Cordero-Morales, J F.]] |
| - | [[Category: Cortes, D | + | [[Category: Cortes, D M.]] |
| - | [[Category: Cuello, L | + | [[Category: Cuello, L G.]] |
[[Category: Jogini, V.]] | [[Category: Jogini, V.]] | ||
[[Category: Perozo, E.]] | [[Category: Perozo, E.]] | ||
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[[Category: x-ray crystallography; potassium ion channel; transmembrane protein]] | [[Category: x-ray crystallography; potassium ion channel; transmembrane protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:19:45 2008'' |
Revision as of 14:19, 21 February 2008
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Structure of mutant KcsA potassium channel
Overview
We show that in the potassium channel KcsA, proton-dependent activation is followed by an inactivation process similar to C-type inactivation, and this process is suppressed by an E71A mutation in the pore helix. EPR spectroscopy demonstrates that the inner gate opens maximally at low pH regardless of the magnitude of the single-channel-open probability, implying that stationary gating originates mostly from rearrangements at the selectivity filter. Two E71A crystal structures obtained at 2.5 A reveal large structural excursions of the selectivity filter during ion conduction and provide a glimpse of the range of conformations available to this region of the channel during gating. These data establish a mechanistic basis for the role of the selectivity filter during channel activation and inactivation.
About this Structure
1ZWI is a Single protein structure of sequence from Mus musculus and Streptomyces lividans with , and as ligands. Full crystallographic information is available from OCA.
Reference
Molecular determinants of gating at the potassium-channel selectivity filter., Cordero-Morales JF, Cuello LG, Zhao Y, Jogini V, Cortes DM, Roux B, Perozo E, Nat Struct Mol Biol. 2006 Apr;13(4):311-8. Epub 2006 Mar 12. PMID:16532009
Page seeded by OCA on Thu Feb 21 16:19:45 2008
