1mo8
From Proteopedia
(New page: 200px<br /><applet load="1mo8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mo8" /> '''ATPase'''<br /> ==Overview== The Na,K-ATPas...) |
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| - | [[Image:1mo8.gif|left|200px]]<br /><applet load="1mo8" size=" | + | [[Image:1mo8.gif|left|200px]]<br /><applet load="1mo8" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mo8" /> | caption="1mo8" /> | ||
'''ATPase'''<br /> | '''ATPase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Na,K-ATPase hydrolyzes ATP to drive the coupled extrusion and uptake | + | 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== | ==About this Structure== | ||
| - | 1MO8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with ATP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1MO8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MO8 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sodium/potassium-exchanging ATPase]] | [[Category: Sodium/potassium-exchanging ATPase]] | ||
| - | [[Category: Abrahams, J | + | [[Category: Abrahams, J P.]] |
| - | [[Category: Gloor, S | + | [[Category: Gloor, S M.]] |
[[Category: Guentert, P.]] | [[Category: Guentert, P.]] | ||
[[Category: Hilge, M.]] | [[Category: Hilge, M.]] | ||
[[Category: Siegal, G.]] | [[Category: Siegal, G.]] | ||
| - | [[Category: Vuister, G | + | [[Category: Vuister, G W.]] |
[[Category: ATP]] | [[Category: ATP]] | ||
[[Category: six-stranded]] | [[Category: six-stranded]] | ||
[[Category: twisted beta sheet]] | [[Category: twisted beta sheet]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:57:13 2008'' |
Revision as of 11:57, 21 February 2008
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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 with as ligand. Active as Sodium/potassium-exchanging ATPase, with EC number 3.6.3.9 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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