3kdp
From Proteopedia
(Difference between revisions)
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- | + | ==Crystal structure of the sodium-potassium pump== | |
- | === | + | <StructureSection load='3kdp' size='340' side='right' caption='[[3kdp]], [[Resolution|resolution]] 3.50Å' scene=''> |
- | + | == Structural highlights == | |
+ | <table><tr><td colspan='2'>[[3kdp]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KDP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KDP FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=MF4:TETRAFLUOROMAGNESATE(2-)'>MF4</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=RB:RUBIDIUM+ION'>RB</scene></td></tr> | ||
+ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3b8e|3b8e]], [[3fgo|3fgo]]</td></tr> | ||
+ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Sodium/potassium-exchanging_ATPase Sodium/potassium-exchanging ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.9 3.6.3.9] </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=3kdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kdp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kdp RCSB], [http://www.ebi.ac.uk/pdbsum/3kdp PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kd/3kdp_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </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]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The Na+,K+-ATPase generates electrochemical gradients for sodium and potassium that are vital to animal cells, exchanging three sodium ions for two potassium ions across the plasma membrane during each cycle of ATP hydrolysis. Here we present the X-ray crystal structure at 3.5 A resolution of the pig renal Na+,K+-ATPase with two rubidium ions bound (as potassium congeners) in an occluded state in the transmembrane part of the alpha-subunit. Several of the residues forming the cavity for rubidium/potassium occlusion in the Na+,K+-ATPase are homologous to those binding calcium in the Ca2+-ATPase of sarco(endo)plasmic reticulum. The beta- and gamma-subunits specific to the Na+,K+-ATPase are associated with transmembrane helices alphaM7/alphaM10 and alphaM9, respectively. The gamma-subunit corresponds to a fragment of the V-type ATPase c subunit. The carboxy terminus of the alpha-subunit is contained within a pocket between transmembrane helices and seems to be a novel regulatory element controlling sodium affinity, possibly influenced by the membrane potential. | ||
- | + | Crystal structure of the sodium-potassium pump.,Morth JP, Pedersen BP, Toustrup-Jensen MS, Sorensen TL, Petersen J, Andersen JP, Vilsen B, Nissen P Nature. 2007 Dec 13;450(7172):1043-9. PMID:18075585<ref>PMID:18075585</ref> | |
- | + | ||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
==See Also== | ==See Also== | ||
*[[ATPase|ATPase]] | *[[ATPase|ATPase]] | ||
- | + | == References == | |
- | + | <references/> | |
- | == | + | __TOC__ |
- | < | + | </StructureSection> |
[[Category: Sodium/potassium-exchanging ATPase]] | [[Category: Sodium/potassium-exchanging ATPase]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
- | [[Category: Morth, J P | + | [[Category: Morth, J P]] |
- | [[Category: Nissen, P | + | [[Category: Nissen, P]] |
- | [[Category: Pedersen, B P | + | [[Category: Pedersen, B P]] |
[[Category: Alpha helical]] | [[Category: Alpha helical]] | ||
[[Category: Atp-binding]] | [[Category: Atp-binding]] |
Revision as of 06:33, 18 December 2014
Crystal structure of the sodium-potassium pump
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Categories: Sodium/potassium-exchanging ATPase | Sus scrofa | Morth, J P | Nissen, P | Pedersen, B P | Alpha helical | Atp-binding | Disulfide bond | Glycoprotein | Heterotrimeric membrane protein complex | Hydrolase | Ion transport | Magnesium | Membrane | Metal-binding | Nucleotide-binding | Phosphoprotein | Potassium | Potassium transport | Signal-anchor | Sodium transport | Sodium/potassium transport | Transmembrane | Transport