5aw2: Difference between revisions

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==Kinetics by X-ray crystallography: Tl+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 85 min==
==Kinetics by X-ray crystallography: Tl+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 85 min==
<StructureSection load='5aw2' size='340' side='right' caption='[[5aw2]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<StructureSection load='5aw2' size='340' side='right'caption='[[5aw2]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5aw2]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Squalus_acanthias Squalus acanthias]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AW2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AW2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5aw2]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Squalus_acanthias Squalus acanthias]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AW2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AW2 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=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MF4:TETRAFLUOROMAGNESATE(2-)'>MF4</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=TL:THALLIUM+(I)+ION'>TL</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]] 3.2&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5avq|5avq]], [[5avr|5avr]], [[5avs|5avs]], [[5avt|5avt]], [[5avu|5avu]], [[5avv|5avv]], [[5avw|5avw]], [[5avx|5avx]], [[5avy|5avy]], [[5avz|5avz]], [[5aw0|5aw0]], [[5aw1|5aw1]], [[5aw3|5aw3]], [[5aw4|5aw4]], [[5aw5|5aw5]], [[5aw6|5aw6]], [[5aw7|5aw7]], [[5aw8|5aw8]], [[5aw9|5aw9]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MF4:TETRAFLUOROMAGNESATE(2-)'>MF4</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=TL:THALLIUM+(I)+ION'>TL</scene></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=5aw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aw2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5aw2 RCSB], [http://www.ebi.ac.uk/pdbsum/5aw2 PDBsum]</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=5aw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aw2 OCA], [https://pdbe.org/5aw2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5aw2 RCSB], [https://www.ebi.ac.uk/pdbsum/5aw2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5aw2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/C4IX13_SQUAC C4IX13_SQUAC]] 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:RU004369]  
[https://www.uniprot.org/uniprot/Q4H132_SQUAC Q4H132_SQUAC]  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 5aw2" style="background-color:#fffaf0;"></div>
==See Also==
*[[ATPase 3D structures|ATPase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Squalus acanthias]]
[[Category: Squalus acanthias]]
[[Category: Cornelius, F]]
[[Category: Cornelius F]]
[[Category: Hirata, A]]
[[Category: Hirata A]]
[[Category: Ogawa, H]]
[[Category: Ogawa H]]
[[Category: Toyoshima, C]]
[[Category: Toyoshima C]]
[[Category: Atp-binding]]
[[Category: Atpase]]
[[Category: Haloacid dehydrogenease superfamily]]
[[Category: Hydrolase]]
[[Category: Hydrolase-transport protein complex]]
[[Category: Ion pump]]
[[Category: Ion transport]]
[[Category: K+ binding]]
[[Category: Kinetic]]
[[Category: Membrane protein]]
[[Category: Nucleotide-binding]]
[[Category: Phosphate analogue]]
[[Category: Phosphoprotein]]

Latest revision as of 18:49, 8 November 2023

Kinetics by X-ray crystallography: Tl+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 85 minKinetics by X-ray crystallography: Tl+-substitution of bound K+ in the E2.MgF42-.2K+ crystal after 85 min

Structural highlights

5aw2 is a 3 chain structure with sequence from Squalus acanthias. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.2Å
Ligands:, , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q4H132_SQUAC

Publication Abstract from PubMed

Na(+),K(+)-ATPase transfers three Na(+) from the cytoplasm into the extracellular medium and two K(+) in the opposite direction per ATP hydrolysed. The binding and release of Na(+) and K(+) are all thought to occur sequentially. Here we demonstrate by X-ray crystallography of the ATPase in E2.MgF4(2-).2K(+), a state analogous to E2.Pi.2K(+), combined with isotopic measurements, that the substitution of the two K(+) with congeners in the extracellular medium indeed occurs at different rates, substantially faster at site II. An analysis of thermal movements of protein atoms in the crystal shows that the M3-M4E helix pair opens and closes the ion pathway leading to the extracellular medium, allowing K(+) at site II to be substituted first. Taken together, these results indicate that site I K(+) is the first cation to bind to the empty cation-binding sites after releasing three Na(+).

Sequential substitution of K(+) bound to Na(+),K(+)-ATPase visualized by X-ray crystallography.,Ogawa H, Cornelius F, Hirata A, Toyoshima C Nat Commun. 2015 Aug 10;6:8004. doi: 10.1038/ncomms9004. PMID:26258479[1]

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

See Also

References

  1. Ogawa H, Cornelius F, Hirata A, Toyoshima C. Sequential substitution of K(+) bound to Na(+),K(+)-ATPase visualized by X-ray crystallography. Nat Commun. 2015 Aug 10;6:8004. doi: 10.1038/ncomms9004. PMID:26258479 doi:http://dx.doi.org/10.1038/ncomms9004

5aw2, resolution 3.20Å

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