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| | <StructureSection load='4xe5' size='340' side='right'caption='[[4xe5]], [[Resolution|resolution]] 3.90Å' scene=''> | | <StructureSection load='4xe5' size='340' side='right'caption='[[4xe5]], [[Resolution|resolution]] 3.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4xe5]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XE5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XE5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4xe5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XE5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XE5 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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OBN:OUABAIN'>OBN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.901Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BFD:ASPARTATE+BERYLLIUM+TRIFLUORIDE'>BFD</scene>, <scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OBN:OUABAIN'>OBN</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4xe5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xe5 OCA], [https://pdbe.org/4xe5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xe5 RCSB], [https://www.ebi.ac.uk/pdbsum/4xe5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xe5 ProSAT]</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=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] | + | [https://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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Bos taurus]] | | [[Category: Bos taurus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Sodium/potassium-exchanging ATPase]]
| + | [[Category: Fedosova NU]] |
| - | [[Category: Fedosova, N U]] | + | [[Category: Gregersen JL]] |
| - | [[Category: Gregersen, J L]] | + | [[Category: Mattle D]] |
| - | [[Category: Mattle, D]] | + | [[Category: Nissen P]] |
| - | [[Category: Nissen, P]] | + | [[Category: Reinhard L]] |
| - | [[Category: Reinhard, L]] | + | |
| - | [[Category: Alpha-helical transmembrane protein]]
| + | |
| - | [[Category: Atp binding]]
| + | |
| - | [[Category: Atpase]]
| + | |
| - | [[Category: Beryllium trifluoride]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Multisubunit complex]]
| + | |
| - | [[Category: Plasma membrane]]
| + | |
| - | [[Category: Potassium ion transport]]
| + | |
| - | [[Category: Receptor for cardiotonic steroid]]
| + | |
| - | [[Category: Sodium binding]]
| + | |
| - | [[Category: Sodium ion transport]]
| + | |
| Structural highlights
Function
ATNG_BOVIN May be involved in forming the receptor site for cardiac glycoside binding or may modulate the transport function of the sodium ATPase.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gregersen JL, Mattle D, Fedosova NU, Nissen P, Reinhard L. Isolation, crystallization and crystal structure determination of bovine kidney Na(+),K(+)-ATPase. Acta Crystallogr F Struct Biol Commun. 2016 Apr 1;72(Pt 4):282-7. doi:, 10.1107/S2053230X1600279X. Epub 2016 Mar 16. PMID:27050261 doi:http://dx.doi.org/10.1107/S2053230X1600279X
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