1mo8

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|PDB= 1mo8 |SIZE=350|CAPTION= <scene name='initialview01'>1mo8</scene>
|PDB= 1mo8 |SIZE=350|CAPTION= <scene name='initialview01'>1mo8</scene>
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>
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|LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>
|ACTIVITY= [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]
|ACTIVITY= [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]
|GENE=
|GENE=
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[[Category: twisted beta sheet]]
[[Category: twisted beta sheet]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:45:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 12:47:17 2008''

Revision as of 10:47, 23 March 2008


PDB ID 1mo8

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Ligands:
Activity: Sodium/potassium-exchanging ATPase, with EC number 3.6.3.9
Coordinates: save as pdb, mmCIF, xml



ATPase


Overview

The Na,K-ATPase hydrolyzes ATP to drive the coupled extrusion and uptake of Na+ and K+ ions across the plasma membrane. Here, we report two high-resolution NMR structures of the 213-residue nucleotide-binding domain of rat alpha1 Na,K-ATPase, determined in the absence and the presence of ATP. The nucleotide binds in the anti conformation and shows a relative paucity of interactions with the protein, reflecting the low-affinity ATP-binding state. Binding of ATP induces substantial conformational changes in the binding pocket and in residues located in the hinge region connecting the N- and P-domains. Structural comparison with the Ca-ATPase stabilized by the inhibitor thapsigargin, E2(TG), and the model of the H-ATPase in the E1 form suggests that the observed changes may trigger the series of events necessary for the release of the K+ ions and/or disengagement of the A-domain, leading to the eventual transfer of the gamma-phosphate group to the invariant Asp369.

About this Structure

1MO8 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase., Hilge M, Siegal G, Vuister GW, Guntert P, Gloor SM, Abrahams JP, Nat Struct Biol. 2003 Jun;10(6):468-74. PMID:12730684

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