1u12
From Proteopedia
(New page: 200px<br /><applet load="1u12" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u12, resolution 2.70Å" /> '''M. loti cyclic nucle...) |
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- | [[Image:1u12.gif|left|200px]]<br /><applet load="1u12" size=" | + | [[Image:1u12.gif|left|200px]]<br /><applet load="1u12" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1u12, resolution 2.70Å" /> | caption="1u12, resolution 2.70Å" /> | ||
'''M. loti cyclic nucleotide binding domain mutant'''<br /> | '''M. loti cyclic nucleotide binding domain mutant'''<br /> | ||
==Overview== | ==Overview== | ||
- | Here we describe the initial functional characterization of a cyclic | + | Here we describe the initial functional characterization of a cyclic nucleotide regulated ion channel from the bacterium Mesorhizobium loti and present two structures of its cyclic nucleotide binding domain, with and without cAMP. The domains are organized as dimers with the interface formed by the linker regions that connect the nucleotide binding pocket to the pore domain. Together, structural and functional data suggest the domains form two dimers on the cytoplasmic face of the channel. We propose a model for gating in which ligand binding alters the structural relationship within a dimer, directly affecting the position of the adjacent transmembrane helices. |
==About this Structure== | ==About this Structure== | ||
- | 1U12 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mesorhizobium_loti_maff303099 Mesorhizobium loti maff303099] with IOD, SO4 and K as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1U12 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mesorhizobium_loti_maff303099 Mesorhizobium loti maff303099] with <scene name='pdbligand=IOD:'>IOD</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=K:'>K</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U12 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mesorhizobium loti maff303099]] | [[Category: Mesorhizobium loti maff303099]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
- | [[Category: Clayton, G | + | [[Category: Clayton, G M.]] |
[[Category: Heginbotham, L.]] | [[Category: Heginbotham, L.]] | ||
- | [[Category: Morais-Cabral, J | + | [[Category: Morais-Cabral, J H.]] |
- | [[Category: Silverman, W | + | [[Category: Silverman, W R.]] |
[[Category: IOD]] | [[Category: IOD]] | ||
[[Category: K]] | [[Category: K]] | ||
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[[Category: unliganded]] | [[Category: unliganded]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:19:29 2008'' |
Revision as of 13:19, 21 February 2008
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M. loti cyclic nucleotide binding domain mutant
Overview
Here we describe the initial functional characterization of a cyclic nucleotide regulated ion channel from the bacterium Mesorhizobium loti and present two structures of its cyclic nucleotide binding domain, with and without cAMP. The domains are organized as dimers with the interface formed by the linker regions that connect the nucleotide binding pocket to the pore domain. Together, structural and functional data suggest the domains form two dimers on the cytoplasmic face of the channel. We propose a model for gating in which ligand binding alters the structural relationship within a dimer, directly affecting the position of the adjacent transmembrane helices.
About this Structure
1U12 is a Single protein structure of sequence from Mesorhizobium loti maff303099 with , and as ligands. Full crystallographic information is available from OCA.
Reference
Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel., Clayton GM, Silverman WR, Heginbotham L, Morais-Cabral JH, Cell. 2004 Nov 24;119(5):615-27. PMID:15550244
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