2jiz

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|PDB= 2jiz |SIZE=350|CAPTION= <scene name='initialview01'>2jiz</scene>, resolution 2.30&Aring;
|PDB= 2jiz |SIZE=350|CAPTION= <scene name='initialview01'>2jiz</scene>, resolution 2.30&Aring;
|SITE= <scene name='pdbsite=AC1:Stl+Binding+Site+For+Chain+N'>AC1</scene>
|SITE= <scene name='pdbsite=AC1:Stl+Binding+Site+For+Chain+N'>AC1</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=STL:RESVERATROL'>STL</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=STL:RESVERATROL'>STL</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
|ACTIVITY= [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]
|ACTIVITY= [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]
|GENE=
|GENE=
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[[Category: transport]]
[[Category: transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:42:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 15:26:51 2008''

Revision as of 13:26, 23 March 2008

Image:2jiz.jpg


PDB ID 2jiz

Drag the structure with the mouse to rotate
, resolution 2.30Å
Sites:
Ligands: , , , , , and
Activity: Transferred entry: 3.6.3.14, with EC number 3.6.1.34
Coordinates: save as pdb, mmCIF, xml



THE STRUCTURE OF F1-ATPASE INHIBITED BY RESVERATROL.


Overview

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.

About this Structure

2JIZ is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

Reference

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

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