2v7q

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[[Image:2v7q.jpg|left|200px]]
[[Image:2v7q.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2v7q |SIZE=350|CAPTION= <scene name='initialview01'>2v7q</scene>, resolution 2.10&Aring;
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The line below this paragraph, containing "STRUCTURE_2v7q", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+F'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosine-tetraphosphatase Adenosine-tetraphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.14 3.6.1.14] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_2v7q| PDB=2v7q | SCENE= }}
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|RELATEDENTRY=[[1bmf|1BMF]], [[1e1q|1E1Q]], [[1e1r|1E1R]], [[1e79|1E79]], [[1h8e|1H8E]], [[1h8h|1H8H]], [[1w0j|1W0J]], [[2jdi|2JDI]], [[2jj1|2JJ1]], [[2jj2|2JJ2]], [[2uys|2UYS]], [[1cow|1COW]], [[1efr|1EFR]], [[1nbm|1NBM]], [[1ohh|1OHH]], [[1qo1|1QO1]], [[1w0k|1W0K]], [[2ck3|2CK3]], [[2jiz|2JIZ]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v7q OCA], [http://www.ebi.ac.uk/pdbsum/2v7q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2v7q RCSB]</span>
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}}
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'''THE STRUCTURE OF F1-ATPASE INHIBITED BY I1-60HIS, A MONOMERIC FORM OF THE INHIBITOR PROTEIN, IF1.'''
'''THE STRUCTURE OF F1-ATPASE INHIBITED BY I1-60HIS, A MONOMERIC FORM OF THE INHIBITOR PROTEIN, IF1.'''
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[[Category: Montgomery, M G.]]
[[Category: Montgomery, M G.]]
[[Category: Walker, J E.]]
[[Category: Walker, J E.]]
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[[Category: acetylation]]
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[[Category: Acetylation]]
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[[Category: alternative splicing]]
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[[Category: Alternative splicing]]
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[[Category: atp synthesis]]
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[[Category: Atp synthesis]]
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[[Category: atp-binding]]
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[[Category: Atp-binding]]
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[[Category: bovine]]
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[[Category: Bovine]]
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[[Category: cf(1)]]
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[[Category: Coiled coil]]
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[[Category: coiled coil]]
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[[Category: F1-atpase]]
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[[Category: f1-atpase]]
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[[Category: Hydrogen ion transport]]
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[[Category: hydrogen ion transport]]
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[[Category: Hydrolase]]
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[[Category: hydrolase]]
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[[Category: Hydrolysis]]
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[[Category: hydrolysis]]
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[[Category: Inhibitor protein]]
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[[Category: inhibitor protein]]
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[[Category: Ion transport]]
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[[Category: ion transport]]
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[[Category: Mitochondrial]]
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[[Category: mitochondrial]]
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[[Category: Mitochondrion]]
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[[Category: mitochondrion]]
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[[Category: Nucleotide-binding]]
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[[Category: nucleotide-binding]]
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[[Category: Pyrrolidone carboxylic acid]]
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[[Category: pyrrolidone carboxylic acid]]
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[[Category: Transit peptide]]
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[[Category: transit peptide]]
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[[Category: Transport]]
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[[Category: transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:20:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:09:17 2008''
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Revision as of 15:20, 4 May 2008

Template:STRUCTURE 2v7q

THE STRUCTURE OF F1-ATPASE INHIBITED BY I1-60HIS, A MONOMERIC FORM OF THE INHIBITOR PROTEIN, IF1.


Overview

The structure of bovine F(1)-ATPase inhibited by a monomeric form of the inhibitor protein, IF(1), known as I1-60His, lacking most of the dimerization region, has been determined at 2.1-A resolution. The resolved region of the inhibitor from residues 8-50 consists of an extended structure from residues 8-13, followed by two alpha-helices from residues 14-18 and residues 21-50 linked by a turn. The binding site in the beta(DP)-alpha(DP) catalytic interface is complex with contributions from five different subunits of F(1)-ATPase. The longer helix extends from the external surface of F(1) via a deep groove made from helices and loops in the C-terminal domains of subunits beta(DP), alpha(DP), beta(TP), and alpha(TP) to the internal cavity surrounding the central stalk. The linker and shorter helix interact with the gamma-subunit in the central stalk, and the N-terminal region extends across the central cavity to interact with the nucleotide binding domain of the alpha(E) subunit. To form these complex interactions and penetrate into the core of the enzyme, it is likely that the initial interaction of the inhibitor with F(1) forms via the open conformation of the beta(E) subunit. Then, as two ATP molecules are hydrolyzed, the beta(E)-alpha(E) interface converts to the beta(DP)-alpha(DP) interface via the beta(TP)-alpha(TP) interface, trapping the inhibitor progressively in its binding site and a nucleotide in the catalytic site of subunit beta(DP). The inhibition probably arises by IF(1) imposing the structure and properties of the beta(TP)-alpha(TP) interface on the beta(DP)-alpha(DP) interface, thereby preventing it from hydrolyzing the bound ATP.

About this Structure

2V7Q is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

Reference

How the regulatory protein, IF(1), inhibits F(1)-ATPase from bovine mitochondria., Gledhill JR, Montgomery MG, Leslie AG, Walker JE, Proc Natl Acad Sci U S A. 2007 Oct 2;104(40):15671-6. Epub 2007 Sep 25. PMID:17895376 Page seeded by OCA on Sun May 4 18:20:17 2008

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