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3n23

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Revision as of 07:12, 23 December 2016

Crystal structure of the high affinity complex between ouabain and the E2P form of the sodium-potassium pump

Structural highlights

3n23 is a 6 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Related:	3kdp, 3b9b, 3n2f
Activity:	Sodium/potassium-exchanging ATPase, with EC number 3.6.3.9
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[AT1A1_PIG] This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients. [AT1B1_PIG] This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane.

Publication Abstract from PubMed

The Na+,K+-ATPase belongs to the P-ATPase family, whose characteristic property is the formation of a phosphorylated intermediate. The enzyme is also a defined target for cardiotonic steroids which inhibit its functional activity and initiate intracellular signaling. Here we describe the 4.6 A resolution crystal structure of the pig kidney Na+,K+-ATPase in its phosphorylated form stabilized by high affinity binding of the cardiotonic steroid ouabain. The steroid binds to a site formed at transmembrane segments alphaM1-alphaM6, plugging the ion pathway from the extracellular side. This structure differs from the previously reported low affinity complex with potassium. Most importantly, the A domain has rotated in response to phosphorylation and alphaM1-2 move towards the ouabain molecule, providing for high affinity interactions and closing the ion pathway from the extracellular side. The observed re-arrangements of the Na+,K+-ATPase stabilized by cardiotonic steroids may affect protein-protein interactions within the intracellular signal transduction networks.

Structural insights into the high affinity binding of cardiotonic steroids to the Na+,K+-ATPase.,Yatime L, Laursen M, Morth JP, Esmann M, Nissen P, Fedosova NU J Struct Biol. 2011 May;174(2):296-306. doi: 10.1016/j.jsb.2010.12.004. Epub 2010, Dec 21. PMID:21182963^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Yatime L, Laursen M, Morth JP, Esmann M, Nissen P, Fedosova NU. Structural insights into the high affinity binding of cardiotonic steroids to the Na+,K+-ATPase. J Struct Biol. 2011 May;174(2):296-306. doi: 10.1016/j.jsb.2010.12.004. Epub 2010, Dec 21. PMID:21182963 doi:http://dx.doi.org/10.1016/j.jsb.2010.12.004

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3n23"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the high affinity complex between ouabain and the E2P form of the sodium-potassium pump==
 <StructureSection load='3n23' size='340' side='right' caption='[[3n23]], [[Resolution|resolution]] 4.60&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kdp|3kdp]], [[3b9b|3b9b]], [[3n2f|3n2f]]</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=3n23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n23 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3n23 RCSB], [http://www.ebi.ac.uk/pdbsum/3n23 PDBsum]</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=3n23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n23 OCA], [http://pdbe.org/3n23 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3n23 RCSB], [http://www.ebi.ac.uk/pdbsum/3n23 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3n23 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 19: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3n23" style="background-color:#fffaf0;"></div>
 ==See Also==

3n23

From Proteopedia

Revision as of 07:12, 23 December 2016

Crystal structure of the high affinity complex between ouabain and the E2P form of the sodium-potassium pump

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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