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1BSN

SOLUTION STRUCTURE OF THE EPSILON SUBUNIT OF THE F1-ATPSYNTHASE FROM ESCHERICHIA COLI AND ORIENTATION OF THE SUBUNIT RELATIVE TO THE BETA SUBUNITS OF THE COMPLEX

1BSN の概要
エントリーDOI10.2210/pdb1bsn/pdb
関連するPDBエントリー1BSH
分子名称PROTEIN (EPSILON SUBUNIT) (1 entity in total)
機能のキーワードatpsynthase, f1-atpase, epsilon subunit, nmr spectroscopy, hydrolase
由来する生物種Escherichia coli
タンパク質・核酸の鎖数1
化学式量合計14956.05
構造登録者
Wilkens, S.,Capaldi, R.A. (登録日: 1998-08-28, 公開日: 1998-09-02, 最終更新日: 2024-04-10)
主引用文献Wilkens, S.,Capaldi, R.A.
Solution structure of the epsilon subunit of the F1-ATPase from Escherichia coli and interactions of this subunit with beta subunits in the complex.
J.Biol.Chem., 273:26645-26651, 1998
Cited by
PubMed Abstract: The solution structure of the epsilon subunit of the Escherichia coli F1-ATPase has been determined by NMR spectroscopy. This subunit has a two-domain structure with an N-terminal 10-stranded beta sandwich and a C-terminal antiparallel two alpha-helix hairpin, as described previously (Wilkens, S., Dahlquist, F. W., McIntosh, L. P., Donaldson, L. W., and Capaldi, R. A. (1995) Nat. Struct. Biol. 2, 961-967). New data show that the two domains interact in solution in an interface formed by beta strand 7 and the very C-terminal alpha-helix. This interface involves only hydrophobic interactions. The dynamics of the epsilon subunit in solution were examined. The two domains are relatively tightly associated with little or no flexibility relative to one another. The epsilon subunit can exist in two states in the ECF1F0 complex depending on whether ATP or ADP occupies catalytic sites. Proteolysis of the epsilon subunit in solution and when bound to the core F1 complex indicates that the conformation of the polypeptide in solution closely resembles the conformation of epsilon when bound to the F1 in the ADP state. Chemical and photo-cross-linking show that the epsilon subunit spans and interacts with two beta subunits in the ADP state. These interactions are disrupted on binding of ATP + Mg2+, as is the interaction between the N- and C-terminal domains of the epsilon subunit.
PubMed: 9756905
DOI: 10.1074/jbc.273.41.26645
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実験手法
SOLUTION NMR
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件を2025-12-31に公開中

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