3co2
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3co2]] is a 4 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3CO2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[3co2]] is a 4 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3CO2 FirstGlance]. <br> | ||
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> |
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3co2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3co2 OCA], [https://pdbe.org/3co2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3co2 RCSB], [https://www.ebi.ac.uk/pdbsum/3co2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3co2 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3co2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3co2 OCA], [https://pdbe.org/3co2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3co2 RCSB], [https://www.ebi.ac.uk/pdbsum/3co2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3co2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/CNGK1_RHILO CNGK1_RHILO] Cyclic nucleotide-regulated potassium channel activated by cAMP.<ref>PMID:15550244</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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/main_output.php?pdb_ID=3co2 ConSurf]. | </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/main_output.php?pdb_ID=3co2 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == 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. | ||
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| - | 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> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3co2" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Mesorhizobium loti]] | [[Category: Mesorhizobium loti]] | ||
| - | [[Category: Alteiri | + | [[Category: Alteiri SL]] |
| - | [[Category: Clayton | + | [[Category: Clayton GM]] |
| - | [[Category: Morais-Cabral | + | [[Category: Morais-Cabral JH]] |
| - | [[Category: Thomas | + | [[Category: Thomas LR]] |
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Current revision
Mlotik1 ion channel cyclic-nucleotide binding domain mutant
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