4aqr
From Proteopedia
(Difference between revisions)
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- | [[ | + | ==Crystal structure of calmodulin in complex with the regulatory domain of a plasma-membrane Ca2+-ATPase== |
+ | <StructureSection load='4aqr' size='340' side='right' caption='[[4aqr]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4aqr]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AQR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AQR FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
+ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Calcium-transporting_ATPase Calcium-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.8 3.6.3.8] </span></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=4aqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aqr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4aqr RCSB], [http://www.ebi.ac.uk/pdbsum/4aqr PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Calcium ions (Ca(2+)) have an important role as secondary messengers in numerous signal transduction processes, and cells invest much energy in controlling and maintaining a steep gradient between intracellular ( approximately 0.1-micromolar) and extracellular ( approximately 2-millimolar) Ca(2+) concentrations. Calmodulin-stimulated calcium pumps, which include the plasma-membrane Ca(2+)-ATPases (PMCAs), are key regulators of intracellular Ca(2+) in eukaryotes. They contain a unique amino- or carboxy-terminal regulatory domain responsible for autoinhibition, and binding of calcium-loaded calmodulin to this domain releases autoinhibition and activates the pump. However, the structural basis for the activation mechanism is unknown and a key remaining question is how calmodulin-mediated PMCA regulation can cover both basal Ca(2+) levels in the nanomolar range as well as micromolar-range Ca(2+) transients generated by cell stimulation. Here we present an integrated study combining the determination of the high-resolution crystal structure of a PMCA regulatory-domain/calmodulin complex with in vivo characterization and biochemical, biophysical and bioinformatics data that provide mechanistic insights into a two-step PMCA activation mechanism mediated by calcium-loaded calmodulin. The structure shows the entire PMCA regulatory domain and reveals an unexpected 2:1 stoichiometry with two calcium-loaded calmodulin molecules binding to different sites on a long helix. A multifaceted characterization of the role of both sites leads to a general structural model for calmodulin-mediated regulation of PMCAs that allows stringent, highly responsive control of intracellular calcium in eukaryotes, making it possible to maintain a stable, basal level at a threshold Ca(2+) concentration, where steep activation occurs. | ||
- | + | A bimodular mechanism of calcium control in eukaryotes.,Tidow H, Poulsen LR, Andreeva A, Knudsen M, Hein KL, Wiuf C, Palmgren MG, Nissen P Nature. 2012 Oct 21. doi: 10.1038/nature11539. PMID:23086147<ref>PMID:23086147</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | == | + | __TOC__ |
- | + | </StructureSection> | |
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: Calcium-transporting ATPase]] | [[Category: Calcium-transporting ATPase]] | ||
- | [[Category: Andreeva, A | + | [[Category: Andreeva, A]] |
- | [[Category: Hein, K L | + | [[Category: Hein, K L]] |
- | [[Category: Nissen, P | + | [[Category: Nissen, P]] |
- | [[Category: Palmgren, M G | + | [[Category: Palmgren, M G]] |
- | [[Category: Poulsen, L R | + | [[Category: Poulsen, L R]] |
- | [[Category: Tidow, H | + | [[Category: Tidow, H]] |
[[Category: Ca-binding protein-hydrolase complex]] | [[Category: Ca-binding protein-hydrolase complex]] | ||
[[Category: Plasma-membrane calcium atpase]] | [[Category: Plasma-membrane calcium atpase]] |
Revision as of 15:16, 9 December 2014
Crystal structure of calmodulin in complex with the regulatory domain of a plasma-membrane Ca2+-ATPase
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