4xe5

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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BFD:ASPARTATE+BERYLLIUM+TRIFLUORIDE'>BFD</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BFD:ASPARTATE+BERYLLIUM+TRIFLUORIDE'>BFD</scene></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='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>
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<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=4xe5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xe5 OCA], [http://pdbe.org/4xe5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xe5 RCSB], [http://www.ebi.ac.uk/pdbsum/4xe5 PDBsum]</span></td></tr>
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<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=4xe5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xe5 OCA], [http://pdbe.org/4xe5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xe5 RCSB], [http://www.ebi.ac.uk/pdbsum/4xe5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xe5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/AT1A1_BOVIN AT1A1_BOVIN]] 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 (By similarity). [[http://www.uniprot.org/uniprot/ATNG_BOVIN ATNG_BOVIN]] May be involved in forming the receptor site for cardiac glycoside binding or may modulate the transport function of the sodium ATPase. [[http://www.uniprot.org/uniprot/G3MWR4_BOVIN G3MWR4_BOVIN]] 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.[RuleBase:RU362099]
[[http://www.uniprot.org/uniprot/AT1A1_BOVIN AT1A1_BOVIN]] 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 (By similarity). [[http://www.uniprot.org/uniprot/ATNG_BOVIN ATNG_BOVIN]] May be involved in forming the receptor site for cardiac glycoside binding or may modulate the transport function of the sodium ATPase. [[http://www.uniprot.org/uniprot/G3MWR4_BOVIN G3MWR4_BOVIN]] 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.[RuleBase:RU362099]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Na(+),K(+)-ATPase is responsible for the transport of Na(+) and K(+) across the plasma membrane in animal cells, thereby sustaining vital electrochemical gradients that energize channels and secondary transporters. The crystal structure of Na(+),K(+)-ATPase has previously been elucidated using the enzyme from native sources such as porcine kidney and shark rectal gland. Here, the isolation, crystallization and first structure determination of bovine kidney Na(+),K(+)-ATPase in a high-affinity E2-BeF3(-)-ouabain complex with bound magnesium are described. Crystals belonging to the orthorhombic space group C2221 with one molecule in the asymmetric unit exhibited anisotropic diffraction to a resolution of 3.7 A with full completeness to a resolution of 4.2 A. The structure was determined by molecular replacement, revealing unbiased electron-density features for bound BeF3(-), ouabain and Mg(2+) ions.
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Isolation, crystallization and crystal structure determination of bovine kidney Na(+),K(+)-ATPase.,Gregersen JL, Mattle D, Fedosova NU, Nissen P, Reinhard L Acta Crystallogr F Struct Biol Commun. 2016 Apr 1;72(Pt 4):282-7. doi:, 10.1107/S2053230X1600279X. Epub 2016 Mar 16. PMID:27050261<ref>PMID:27050261</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4xe5" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 06:34, 26 July 2016

Crystal structure of the Na,K-ATPase from bovine

4xe5, resolution 3.90Å

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