1VP6

M.loti ion channel cylic nucleotide binding domain

Replaces:  1PF0

Summary for 1VP6

• Entry DOI: 10.2210/pdb1vp6/pdb
• Descriptor: Cyclic-nucleotide binding domain of mesorhizobium loti CNG potassium channel, BROMIDE ION, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE, ... (4 entities in total)
• Functional Keywords: dimer helical bundle beta barrel core with cyclic amp bound, membrane protein
• Biological source: Mesorhizobium loti
• Cellular location: Cell membrane; Multi-pass membrane protein: Q98GN8
• Total number of polymer chains: 2
• Total formula weight: 31100.58

Authors

Clayton, G.M.,Silverman, W.R.,Heginbotham, L.,Morais-Cabral, J.H. (deposition date: 2004-10-14, release date: 2004-10-26, Last modification date: 2023-12-27)

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 (1.7 Å)