1qo1: Difference between revisions

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-{{Seed}}
-[[Image:1qo1.png|left|200px]]
-<!--
+==Molecular Architecture of the Rotary Motor in ATP Synthase from Yeast Mitochondria==
-The line below this paragraph, containing "STRUCTURE_1qo1", creates the "Structure Box" on the page.
+<StructureSection load='1qo1' size='340' side='right'caption='[[1qo1]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1qo1]] is a 18 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=1QO1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QO1 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.9&#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=1qo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qo1 OCA], [https://pdbe.org/1qo1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qo1 RCSB], [https://www.ebi.ac.uk/pdbsum/1qo1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qo1 ProSAT]</span></td></tr>
-{{STRUCTURE_1qo1|  PDB=1qo1  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ATPA_BOVIN ATPA_BOVIN] 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. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).
+== 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/qo/1qo1_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=1qo1 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Adenosine triphosphate (ATP) synthase contains a rotary motor involved in biological energy conversion. Its membrane-embedded F0 sector has a rotation generator fueled by the proton-motive force, which provides the energy required for the synthesis of ATP by the F1 domain. An electron density map obtained from crystals of a subcomplex of yeast mitochondrial ATP synthase shows a ring of 10 c subunits. Each c subunit forms an alpha-helical hairpin. The interhelical loops of six to seven of the c subunits are in close contact with the gamma and delta subunits of the central stalk. The extensive contact between the c ring and the stalk suggests that they may rotate as an ensemble during catalysis.
-===MOLECULAR ARCHITECTURE OF THE ROTARY MOTOR IN ATP SYNTHASE FROM YEAST MITOCHONDRIA===
+Molecular architecture of the rotary motor in ATP synthase.,Stock D, Leslie AG, Walker JE Science. 1999 Nov 26;286(5445):1700-5. PMID:10576729<ref>PMID:10576729</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1qo1" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_10576729}}, adds the Publication Abstract to the page
+*[[ATPase 3D structures|ATPase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 10576729 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_10576729}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-QO1 is a 18 chains structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QO1 OCA].
-==Reference==
-<ref group="xtra">PMID:10576729</ref><references group="xtra"/>
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Leslie, A G.W.]]
+[[Category: Leslie AGW]]
-[[Category: Stock, D.]]
+[[Category: Stock D]]
-[[Category: Walker, J E.]]
+[[Category: Walker JE]]
-[[Category: Atp synthase]]
-[[Category: C-alpha only]]
-[[Category: Low resolution model]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 09:23:25 2009''