1u12
From Proteopedia
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|PDB= 1u12 |SIZE=350|CAPTION= <scene name='initialview01'>1u12</scene>, resolution 2.70Å | |PDB= 1u12 |SIZE=350|CAPTION= <scene name='initialview01'>1u12</scene>, resolution 2.70Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1pf0|1PF0]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u12 OCA], [http://www.ebi.ac.uk/pdbsum/1u12 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1u12 RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Morais-Cabral, J H.]] | [[Category: Morais-Cabral, J H.]] | ||
[[Category: Silverman, W R.]] | [[Category: Silverman, W R.]] | ||
| - | [[Category: IOD]] | ||
| - | [[Category: K]] | ||
| - | [[Category: SO4]] | ||
[[Category: c-helix mutation]] | [[Category: c-helix mutation]] | ||
[[Category: mutant cyclic nucleotide binding domain]] | [[Category: mutant cyclic nucleotide binding domain]] | ||
[[Category: unliganded]] | [[Category: unliganded]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:03:56 2008'' |
Revision as of 21:03, 30 March 2008
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| , resolution 2.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 1PF0
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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