3clp: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==M. loti cyclic-nucleotide binding domain mutant 2== | ==M. loti cyclic-nucleotide binding domain mutant 2== | ||
<StructureSection load='3clp' size='340' side='right' caption='[[3clp]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='3clp' size='340' side='right'caption='[[3clp]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3clp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhizobium_loti Rhizobium loti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CLP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CLP FirstGlance]. <br> | <table><tr><td colspan='2'>[[3clp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhizobium_loti Rhizobium loti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CLP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CLP FirstGlance]. <br> | ||
| Line 14: | Line 14: | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cl/3clp_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cl/3clp_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
| Line 29: | Line 29: | ||
</div> | </div> | ||
<div class="pdbe-citations 3clp" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3clp" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Ion channels|Ion channels]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Rhizobium loti]] | [[Category: Rhizobium loti]] | ||
[[Category: Altieri, S L]] | [[Category: Altieri, S L]] | ||
Revision as of 10:53, 24 July 2019
M. loti cyclic-nucleotide binding domain mutant 2M. loti cyclic-nucleotide binding domain mutant 2
Structural highlights
Function[CNGK1_RHILO] Cyclic nucleotide-regulated potassium channel activated by cAMP.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMlotiK1 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||