2jiz

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[[Image:2jiz.jpg|left|200px]]<br /><applet load="2jiz" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2jiz, resolution 2.30&Aring;" />
 
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'''THE STRUCTURE OF F1-ATPASE INHIBITED BY RESVERATROL.'''<br />
 
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==Overview==
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==The Structure of F1-ATPase inhibited by resveratrol.==
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The structures of F(1)-ATPase from bovine heart mitochondria inhibited, with the dietary phytopolyphenol, resveratrol, and with the related, polyphenols quercetin and piceatannol have been determined at 2.3-, 2.4-, and 2.7-A resolution, respectively. The inhibitors bind to a common site, in the inside surface of an annulus made from loops in the three alpha-, and three beta-subunits beneath the "crown" of beta-strands in their, N-terminal domains. This region of F(1)-ATPase forms a bearing to allow, the rotation of the tip of the gamma-subunit inside the annulus during, catalysis. The binding site is a hydrophobic pocket between the C-terminal, tip of the gamma-subunit and the beta(TP) subunit, and the inhibitors are, bound via H-bonds mostly to their hydroxyl moieties mediated by bound, water molecules and by hydrophobic interactions. There are no equivalent, sites between the gamma-subunit and either the beta(DP) or the beta(E), subunit. The inhibitors probably prevent both the synthetic and hydrolytic, activities of the enzyme by blocking both senses of rotation of the, gamma-subunit. The beneficial effects of dietary resveratrol may derive in, part by preventing mitochondrial ATP synthesis in tumor cells, thereby, inducing apoptosis.
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<StructureSection load='2jiz' size='340' side='right'caption='[[2jiz]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2jiz]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JIZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JIZ FirstGlance]. <br>
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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]] 2.3&#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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=STL:RESVERATROL'>STL</scene></td></tr>
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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=2jiz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jiz OCA], [https://pdbe.org/2jiz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jiz RCSB], [https://www.ebi.ac.uk/pdbsum/2jiz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jiz ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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).
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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/ji/2jiz_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=2jiz 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 structures of F(1)-ATPase from bovine heart mitochondria inhibited with the dietary phytopolyphenol, resveratrol, and with the related polyphenols quercetin and piceatannol have been determined at 2.3-, 2.4- and 2.7-A resolution, respectively. The inhibitors bind to a common site in the inside surface of an annulus made from loops in the three alpha- and three beta-subunits beneath the "crown" of beta-strands in their N-terminal domains. This region of F(1)-ATPase forms a bearing to allow the rotation of the tip of the gamma-subunit inside the annulus during catalysis. The binding site is a hydrophobic pocket between the C-terminal tip of the gamma-subunit and the beta(TP) subunit, and the inhibitors are bound via H-bonds mostly to their hydroxyl moieties mediated by bound water molecules and by hydrophobic interactions. There are no equivalent sites between the gamma-subunit and either the beta(DP) or the beta(E) subunit. The inhibitors probably prevent both the synthetic and hydrolytic activities of the enzyme by blocking both senses of rotation of the gamma-subunit. The beneficial effects of dietary resveratrol may derive in part by preventing mitochondrial ATP synthesis in tumor cells, thereby inducing apoptosis.
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==About this Structure==
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Mechanism of inhibition of bovine F1-ATPase by resveratrol and related polyphenols.,Gledhill JR, Montgomery MG, Leslie AG, Walker JE Proc Natl Acad Sci U S A. 2007 Aug 21;104(34):13632-7. Epub 2007 Aug 13. PMID:17698806<ref>PMID:17698806</ref>
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2JIZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with MG, AZI, PO4, ANP, ADP, STL and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_3.6.3.14 Transferred entry: 3.6.3.14], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.34 3.6.1.34] Known structural/functional Site: <scene name='pdbsite=AC1:Stl Binding Site For Chain N'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2JIZ OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Mechanism of inhibition of bovine F1-ATPase by resveratrol and related polyphenols., Gledhill JR, Montgomery MG, Leslie AG, Walker JE, Proc Natl Acad Sci U S A. 2007 Aug 21;104(34):13632-7. Epub 2007 Aug 13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17698806 17698806]
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</div>
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[[Category: Bos taurus]]
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<div class="pdbe-citations 2jiz" style="background-color:#fffaf0;"></div>
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[[Category: Protein complex]]
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[[Category: Transferred entry: 3.6.3.14]]
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[[Category: Gledhill, J.R.]]
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[[Category: Leslie, A.G.W.]]
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[[Category: Montgomery, M.G.]]
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[[Category: Walker, J.E.]]
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[[Category: ADP]]
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[[Category: ANP]]
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[[Category: AZI]]
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[[Category: GOL]]
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[[Category: MG]]
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[[Category: PO4]]
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[[Category: STL]]
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[[Category: acetylation]]
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[[Category: alternative splicing]]
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[[Category: atp synthesis]]
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[[Category: atp-binding]]
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[[Category: bovine]]
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[[Category: cf(1)]]
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[[Category: f1-atpase]]
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[[Category: hydrogen ion transport]]
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[[Category: hydrolase]]
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[[Category: hydrolysis]]
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[[Category: ion transport]]
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[[Category: mitochondrial]]
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[[Category: mitochondrion]]
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[[Category: nucleotide-binding]]
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[[Category: pyrrolidone carboxylic acid]]
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[[Category: resveratrol]]
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[[Category: transit peptide]]
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[[Category: transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 20:12:03 2007''
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==See Also==
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*[[ATPase 3D structures|ATPase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bos taurus]]
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[[Category: Large Structures]]
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[[Category: Gledhill JR]]
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[[Category: Leslie AGW]]
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[[Category: Montgomery MG]]
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[[Category: Walker JE]]

Current revision

The Structure of F1-ATPase inhibited by resveratrol.

PDB ID 2jiz

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