7tk4: Difference between revisions

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====
==Yeast ATP synthase State 1binding(c) with 10 mM ATP backbone model==
<StructureSection load='7tk4' size='340' side='right'caption='[[7tk4]]' scene=''>
<StructureSection load='7tk4' size='340' side='right'caption='[[7tk4]], [[Resolution|resolution]] 7.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
<table><tr><td colspan='2'>[[7tk4]] is a 23 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TK4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TK4 FirstGlance]. <br>
</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=7tk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tk4 OCA], [https://pdbe.org/7tk4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tk4 RCSB], [https://www.ebi.ac.uk/pdbsum/7tk4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tk4 ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 7&#8491;</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=7tk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tk4 OCA], [https://pdbe.org/7tk4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tk4 RCSB], [https://www.ebi.ac.uk/pdbsum/7tk4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tk4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ATP9_YEAST ATP9_YEAST] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton 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 proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.
==See Also==
*[[ATPase 3D structures|ATPase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Z-disk]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Guo H]]
[[Category: Rubinstein JL]]

Latest revision as of 13:54, 21 February 2024

Yeast ATP synthase State 1binding(c) with 10 mM ATP backbone modelYeast ATP synthase State 1binding(c) with 10 mM ATP backbone model

Structural highlights

7tk4 is a 23 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 7Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ATP9_YEAST Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton 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 proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.

See Also

7tk4, resolution 7.00Å

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