6cjq

<StructureSection load='6cjq' size='340' side='right'caption='[[6cjq]], [[Resolution|resolution]] 3.42&Aring;' scene=''>

<table><tr><td colspan='2'>[[6cjq]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Spitz Spitz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CJQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CJQ FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PGW:(1R)-2-{[(S)-{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(HEXADECANOYLOXY)METHYL]ETHYL+(9Z)-OCTADEC-9-ENOATE'>PGW</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Spith_0644 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=869211 SPITZ])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6cjq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cjq OCA], [http://pdbe.org/6cjq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cjq RCSB], [http://www.ebi.ac.uk/pdbsum/6cjq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cjq ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Cyclic nucleotide-modulated channels have important roles in visual signal transduction and pacemaking. Binding of cyclic nucleotides (cAMP/cGMP) elicits diverse functional responses in different channels within the family despite their high sequence and structure homology. The molecular mechanisms responsible for ligand discrimination and gating are unknown due to lack of correspondence between structural information and functional states. Using single particle cryo-electron microscopy and single-channel recording, we assigned functional states to high-resolution structures of SthK, a prokaryotic cyclic nucleotide-gated channel. The structures for apo, cAMP-bound, and cGMP-bound SthK in lipid nanodiscs, correspond to no, moderate, and low single-channel activity, respectively, consistent with the observation that all structures are in resting, closed states. The similarity between apo and ligand-bound structures indicates that ligand-binding domains are strongly coupled to pore and SthK gates in an allosteric, concerted fashion. The different orientations of cAMP and cGMP in the 'resting' and 'activated' structures suggest a mechanism for ligand discrimination.

 

<div class="pdbe-citations 6cjq" style="background-color:#fffaf0;"></div>

== References ==

</StructureSection>

[[Category: Spitz]]

[[Category: Nimigean, C M]]

[[Category: Rheinberger, J]]

[[Category: Transport protein]]