3fks

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{{Seed}}
 
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[[Image:3fks.png|left|200px]]
 
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==Yeast F1 ATPase in the absence of bound nucleotides==
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The line below this paragraph, containing "STRUCTURE_3fks", creates the "Structure Box" on the page.
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<StructureSection load='3fks' size='340' side='right'caption='[[3fks]], [[Resolution|resolution]] 3.59&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3fks]] is a 27 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=3FKS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FKS FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.587&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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{{STRUCTURE_3fks| PDB=3fks | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fks OCA], [https://pdbe.org/3fks PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fks RCSB], [https://www.ebi.ac.uk/pdbsum/3fks PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fks ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ATPA_YEAST ATPA_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. 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).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fk/3fks_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=3fks ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The crystal structure of nucleotide-free yeast F(1) ATPase has been determined at a resolution of 3.6 A. The overall structure is very similar to that of the ground state enzyme. In particular, the beta(DP) and beta(TP) subunits both adopt the closed conformation found in the ground state structure despite the absence of bound nucleotides. This implies that interactions between the gamma and beta subunits are as important as nucleotide occupancy in determining the conformational state of the beta subunits. Furthermore, this result suggests that for the mitochondrial enzyme, there is no state of nucleotide occupancy that would result in more than one of the beta subunits adopting the open conformation. The adenine-binding pocket of the beta(TP) subunit is disrupted in the apoenzyme, suggesting that the beta(DP) subunit is responsible for unisite catalytic activity.
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===Yeast F1 ATPase in the absence of bound nucleotides===
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Asymmetric structure of the yeast F1 ATPase in the absence of bound nucleotides.,Kabaleeswaran V, Shen H, Symersky J, Walker JE, Leslie AG, Mueller DM J Biol Chem. 2009 Apr 17;284(16):10546-51. Epub 2009 Feb 20. PMID:19233840<ref>PMID:19233840</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3fks" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19233840}}, adds the Publication Abstract to the page
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*[[ATPase 3D structures|ATPase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19233840 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19233840}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3FKS is a 27 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=3FKS OCA].
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==Reference==
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<ref group="xtra">PMID:19233840</ref><references group="xtra"/>
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Kabaleeswaran, V.]]
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[[Category: Kabaleeswaran V]]
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[[Category: Leslie, A G.W.]]
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[[Category: Leslie AGW]]
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[[Category: Mueller, D M.]]
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[[Category: Mueller DM]]
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[[Category: Shen, H.]]
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[[Category: Shen H]]
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[[Category: Symersky, J.]]
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[[Category: Symersky J]]
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[[Category: Walker, J E.]]
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[[Category: Walker JE]]
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[[Category: Atp phosphatase]]
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[[Category: Atp synthase]]
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[[Category: Atp synthesis]]
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[[Category: Atp-binding]]
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[[Category: F1f0 atpase]]
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[[Category: Hydrogen ion transport]]
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[[Category: Hydrolase]]
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[[Category: Ion transport]]
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[[Category: Membrane]]
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[[Category: Mitochondrion]]
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[[Category: Mitochondrion inner membrane]]
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[[Category: Nucleotide-binding]]
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[[Category: Phosphoprotein]]
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[[Category: Transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 29 20:59:52 2009''
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Current revision

Yeast F1 ATPase in the absence of bound nucleotides

PDB ID 3fks

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