1U12

M. loti cyclic nucleotide binding domain mutant

Summary for 1U12

• Entry DOI: 10.2210/pdb1u12/pdb
• Related: 1PF0
• Descriptor: cyclic nucleotide binding domain, IODIDE ION, SULFATE ION, ... (5 entities in total)
• Functional Keywords: mutant cyclic nucleotide binding domain, c-helix mutation, unliganded, membrane protein
• Biological source: Mesorhizobium loti
• Cellular location: Cell membrane; Multi-pass membrane protein: Q98GN8
• Total number of polymer chains: 2
• Total formula weight: 33274.01

Authors

Clayton, G.M.,Silverman, W.R.,Heginbotham, L.,Morais-Cabral, J.H. (deposition date: 2004-07-14, release date: 2004-11-30, Last modification date: 2024-02-14)

Primary citation

Clayton, G.M.,Silverman, W.R.,Heginbotham, L.,Morais-Cabral, J.H.
Structural Basis of Ligand Activation in a Cyclic Nucleotide Regulated Potassium Channel
Cell(Cambridge,Mass.), 119:615-627, 2004

PubMed Abstract: 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.

PubMed: 15550244
DOI: 10.1016/j.cell.2004.10.030

Experimental method

X-RAY DIFFRACTION (2.7 Å)