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[[Image:1yce.png|left|200px]]


{{STRUCTURE_1yce|  PDB=1yce  |  SCENE=  }}
==Structure of the rotor ring of F-type Na+-ATPase from Ilyobacter tartaricus==
 
<StructureSection load='1yce' size='340' side='right'caption='[[1yce]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
===Structure of the rotor ring of F-type Na+-ATPase from Ilyobacter tartaricus===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[1yce]] is a 44 chain structure with sequence from [https://en.wikipedia.org/wiki/Ilyobacter_tartaricus Ilyobacter tartaricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YCE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YCE FirstGlance]. <br>
{{ABSTRACT_PUBMED_15860619}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F09:NONAN-1-OL'>F09</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yce OCA], [https://pdbe.org/1yce PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yce RCSB], [https://www.ebi.ac.uk/pdbsum/1yce PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yce ProSAT]</span></td></tr>
[[1yce]] is a 44 chain structure with sequence from [http://en.wikipedia.org/wiki/Ilyobacter_tartaricus Ilyobacter tartaricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YCE OCA].  
</table>
== Function ==
[https://www.uniprot.org/uniprot/ATPL_ILYTA ATPL_ILYTA] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane sodium channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to sodium translocation.[HAMAP-Rule:MF_01396]  Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of 11 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.[HAMAP-Rule:MF_01396]
== 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/yc/1yce_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/main_output.php?pdb_ID=1yce ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[ATPase|ATPase]]
*[[ATPase 3D structures|ATPase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
<ref group="xtra">PMID:015860619</ref><references group="xtra"/>
[[Category: Ilyobacter tartaricus]]
[[Category: Ilyobacter tartaricus]]
[[Category: Diederichs, K.]]
[[Category: Large Structures]]
[[Category: Dimroth, P.]]
[[Category: Diederichs K]]
[[Category: Meier, T.]]
[[Category: Dimroth P]]
[[Category: Polzer, P.]]
[[Category: Meier T]]
[[Category: Welte, W.]]
[[Category: Polzer P]]
[[Category: Atp synthase]]
[[Category: Welte W]]
[[Category: Membrane protein]]
[[Category: Na binding site]]