3co2

<StructureSection load='3co2' size='340' side='right' caption='[[3co2]], [[Resolution|resolution]] 2.90&Aring;' scene=''>

<table><tr><td colspan='2'>[[3co2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mesorhizobium_loti Mesorhizobium loti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CO2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CO2 FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vp6|1vp6]], [[1u12|1u12]], [[3cl1|3cl1]], [[3clp|3clp]], [[3beh|3beh]]</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=3co2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3co2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3co2 RCSB], [http://www.ebi.ac.uk/pdbsum/3co2 PDBsum]</span></td></tr>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/co/3co2_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

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== Publication Abstract from PubMed ==

MlotiK1 is a prokaryotic homolog of cyclic-nucleotide-dependent ion channels that contains an intracellular C-terminal cyclic nucleotide binding (CNB) domain. X-ray structures of the CNB domain have been solved in the absence of ligand and bound to cAMP. Both the full-length channel and CNB domain fragment are easily expressed and purified, making MlotiK1 a useful model system for dissecting activation by ligand binding. We have used X-ray crystallography to determine three new MlotiK1 CNB domain structures: a second apo configuration, a cGMP-bound structure, and a second cAMP-bound structure. In combination, the five MlotiK1 CNB domain structures provide a unique opportunity for analyzing, within a single protein, the structural differences between the apo state and the bound state, and the structural variability within each state. With this analysis as a guide, we have probed the nucleotide selectivity and importance of specific residue side chains in ligand binding and channel activation. These data help to identify ligand-protein interactions that are important for ligand dependence in MlotiK1 and, more globally, in the class of nucleotide-dependent proteins.

Structural and energetic analysis of activation by a cyclic nucleotide binding domain.,Altieri SL, Clayton GM, Silverman WR, Olivares AO, De la Cruz EM, Thomas LR, Morais-Cabral JH J Mol Biol. 2008 Sep 5;381(3):655-69. Epub 2008 Jun 10. PMID:18619611<ref>PMID:18619611</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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*[[Ion channels|Ion channels]]

*[[Potassium Channel|Potassium Channel]]

[[Category: Alteiri, S L]]

[[Category: Clayton, G M]]

[[Category: Morais-Cabral, J H]]

[[Category: Thomas, L R]]

[[Category: Unliganded]]