1mo8
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-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= <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=[[1mo7|1MO7]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mo8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mo8 OCA], [http://www.ebi.ac.uk/pdbsum/1mo8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mo8 RCSB]</span> | ||
}} | }} | ||
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[[Category: Siegal, G.]] | [[Category: Siegal, G.]] | ||
[[Category: Vuister, G W.]] | [[Category: Vuister, G W.]] | ||
| - | [[Category: ATP]] | ||
[[Category: six-stranded]] | [[Category: six-stranded]] | ||
[[Category: twisted beta sheet]] | [[Category: twisted beta sheet]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:18:47 2008'' |
Revision as of 19:18, 30 March 2008
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| Ligands: | |||||||
| Activity: | Sodium/potassium-exchanging ATPase, with EC number 3.6.3.9 | ||||||
| Related: | 1MO7
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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