1yce
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == 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> | <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> | ||
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</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> | ||
<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> | <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> | ||
</table> | </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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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]. | </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> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | In the crystal structure of the membrane-embedded rotor ring of the sodium ion-translocating adenosine 5'-triphosphate (ATP) synthase of Ilyobacter tartaricus at 2.4 angstrom resolution, 11 c subunits are assembled into an hourglass-shaped cylinder with 11-fold symmetry. Sodium ions are bound in a locked conformation close to the outer surface of the cylinder near the middle of the membrane. The structure supports an ion-translocation mechanism in the intact ATP synthase in which the binding site converts from the locked conformation into one that opens toward subunit a as the rotor ring moves through the subunit a/c interface. | ||
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| - | Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus.,Meier T, Polzer P, Diederichs K, Welte W, Dimroth P Science. 2005 Apr 29;308(5722):659-62. PMID:15860619<ref>PMID:15860619</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1yce" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[ATPase 3D structures|ATPase 3D structures]] | *[[ATPase 3D structures|ATPase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Ilyobacter tartaricus]] | [[Category: Ilyobacter tartaricus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Diederichs | + | [[Category: Diederichs K]] |
| - | [[Category: Dimroth | + | [[Category: Dimroth P]] |
| - | [[Category: Meier | + | [[Category: Meier T]] |
| - | [[Category: Polzer | + | [[Category: Polzer P]] |
| - | [[Category: Welte | + | [[Category: Welte W]] |
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Current revision
Structure of the rotor ring of F-type Na+-ATPase from Ilyobacter tartaricus
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