1mo7

From Proteopedia

(Difference between revisions)

Current revision

ATPase

Structural highlights

1mo7 is a 1 chain structure with sequence from Rattus norvegicus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AT1A1_RAT This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

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

References

↑ Hilge M, Siegal G, Vuister GW, Guntert P, Gloor SM, Abrahams JP. ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase. Nat Struct Biol. 2003 Jun;10(6):468-74. PMID:12730684 doi:http://dx.doi.org/10.1038/nsb924

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1mo7"

@@ Line 1: / Line 1: @@
 ==ATPase==
-<StructureSection load='1mo7' size='340' side='right' caption='[[1mo7]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1mo7' size='340' side='right'caption='[[1mo7]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mo7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MO7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MO7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mo7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MO7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MO7 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mo8|1mo8]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></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=1mo7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mo7 OCA], [https://pdbe.org/1mo7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mo7 RCSB], [https://www.ebi.ac.uk/pdbsum/1mo7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mo7 ProSAT]</span></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=1mo7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mo7 OCA], [http://pdbe.org/1mo7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mo7 RCSB], [http://www.ebi.ac.uk/pdbsum/1mo7 PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/AT1A1_RAT AT1A1_RAT]] This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients.
+[https://www.uniprot.org/uniprot/AT1A1_RAT AT1A1_RAT] This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mo/1mo7_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mo/1mo7_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mo7 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 30: / Line 30: @@
 ==See Also==
-*[[ATPase|ATPase]]
+*[[ATPase 3D structures|ATPase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Buffalo rat]]
+[[Category: Large Structures]]
-[[Category: Sodium/potassium-exchanging ATPase]]
+[[Category: Rattus norvegicus]]
-[[Category: Abrahams, J P]]
+[[Category: Abrahams JP]]
-[[Category: Gloor, S M]]
+[[Category: Gloor SM]]
-[[Category: Guentert, P]]
+[[Category: Guentert P]]
-[[Category: Hilge, M]]
+[[Category: Hilge M]]
-[[Category: Siegal, G]]
+[[Category: Siegal G]]
-[[Category: Vuister, G W]]
+[[Category: Vuister GW]]
-[[Category: Hydrolase]]
-[[Category: Six-stranded]]
-[[Category: Twisted beta sheet]]

1mo7

From Proteopedia

Current revision

ATPase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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