1mo7: Difference between revisions

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|SITE=  
|SITE=  
|LIGAND=  
|LIGAND=  
|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= <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>
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=[[1mo8|1MO8]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mo7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mo7 OCA], [http://www.ebi.ac.uk/pdbsum/1mo7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mo7 RCSB]</span>
}}
}}


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[[Category: twisted beta sheet]]
[[Category: twisted beta sheet]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:45:58 2008''
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Revision as of 22:18, 30 March 2008

File:1mo7.gif


PDB ID 1mo7

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Activity: Sodium/potassium-exchanging ATPase, with EC number 3.6.3.9
Related: 1MO8


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



ATPase


OverviewOverview

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 StructureAbout this Structure

1MO7 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

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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