1efr
From Proteopedia
(New page: 200px<br /> <applet load="1efr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1efr, resolution 3.1Å" /> '''BOVINE MITOCHONDRIAL...) |
|||
Line 8: | Line 8: | ||
==About this Structure== | ==About this Structure== | ||
- | 1EFR 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, ANP and ADP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.34 3.6.1.34]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EFR OCA]]. | + | 1EFR 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, ANP and ADP 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]]. Structure known Active Sites: CAT and PLP. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EFR OCA]]. |
==Reference== | ==Reference== | ||
Line 14: | Line 14: | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
+ | [[Category: Transferred entry: 3.6.3.14]] | ||
[[Category: Abrahams, J.P.]] | [[Category: Abrahams, J.P.]] | ||
[[Category: Buchanan, S.K.]] | [[Category: Buchanan, S.K.]] | ||
Line 30: | Line 31: | ||
[[Category: hydrogen ion transport]] | [[Category: hydrogen ion transport]] | ||
- | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:41:57 2007'' |
Revision as of 10:37, 30 October 2007
|
BOVINE MITOCHONDRIAL F1-ATPASE COMPLEXED WITH THE PEPTIDE ANTIBIOTIC EFRAPEPTIN
Overview
In the previously determined structure of mitochondrial F1-ATPase, determined with crystals grown in the presence of, adenylyl-imidodiphosphate (AMP-PNP) and ADP, the three catalytic, beta-subunits have different conformations and nucleotide occupancies., AMP-PNP and ADP are bound to subunits beta TP and beta DP, respectively, and the third beta-subunit (beta E) has no bound nucleotide. The, efrapeptins are a closely related family of modified linear peptides, containing 15 amino acids that inhibit both ATP synthesis and hydrolysis, by binding to the F1 catalytic domain of F1F0-ATP synthase. In crystals of, F1-ATPase grown in the presence of both nucleotides and inhibitor, efrapeptin is bound to a unique site in the central cavity of the enzyme., Its binding is associated with small ... [(full description)]
About this Structure
1EFR is a [Protein complex] structure of sequences from [Bos taurus] with MG, ANP and ADP as [ligands]. Active as [Transferred entry: 3.6.3.14], with EC number [3.6.1.34]. Structure known Active Sites: CAT and PLP. Full crystallographic information is available from [OCA].
Reference
The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin., Abrahams JP, Buchanan SK, Van Raaij MJ, Fearnley IM, Leslie AG, Walker JE, Proc Natl Acad Sci U S A. 1996 Sep 3;93(18):9420-4. PMID:8790345
Page seeded by OCA on Tue Oct 30 12:41:57 2007
Categories: Bos taurus | Protein complex | Transferred entry: 3.6.3.14 | Abrahams, J.P. | Buchanan, S.K. | Fearnley, I.M. | Leslie, A.G.W. | Raaij, M.J.Van. | Walker, J.E. | ADP | ANP | MG | Atp phosphorylase | Atp synthase | Complex (ion transport/inhibitor) | F1-atpase | F1f atp synthase | Hydrogen ion transport