2v7q: Difference between revisions
New page: left|200px<br /> <applet load="2v7q" size="450" color="white" frame="true" align="right" spinBox="true" caption="2v7q, resolution 2.10Å" /> '''THE STRUCTURE OF F1... |
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==About this Structure== | ==About this Structure== | ||
2V7Q is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from | 2V7Q 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, PO4, ATP and ADP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[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]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2V7Q OCA]]. | ||
==Reference== | ==Reference== | ||
How the regulatory protein, IF1, inhibits F1-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17895376 17895376] | How the regulatory protein, IF1, inhibits F1-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17895376 17895376] | ||
[[Category: Adenosine-tetraphosphatase]] | |||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: transport]] | [[Category: transport]] | ||
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Revision as of 15:46, 30 October 2007
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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, ... [(full description)]
About this Structure
2V7Q is a [Protein complex] structure of sequences from [Bos taurus] with MG, PO4, ATP and ADP as [ligands]. Active as [Adenosine-tetraphosphatase], with EC number [3.6.1.14]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
How the regulatory protein, IF1, inhibits F1-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
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Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- Adenosine-tetraphosphatase
- Bos taurus
- Protein complex
- Gledhill, J.R.
- Leslie, A.G.W.
- Montgomery, M.G.
- Walker, J.E.
- ADP
- ATP
- MG
- PO4
- Acetylation
- Alternative splicing
- Atp synthesis
- Atp-binding
- Bovine
- Cf(1)
- Coiled coil
- F1-atpase
- Hydrogen ion transport
- Hydrolase
- Hydrolysis
- Inhibitor protein
- Ion transport
- Mitochondrial
- Mitochondrion
- Nucleotide-binding
- Pyrrolidone carboxylic acid
- Transit peptide
- Transport
