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PDBsum entry 2a7u
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References listed in PDB file
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Key reference
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Title
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Structural characterization of the interaction of the delta and alpha subunits of the escherichia coli f1f0-Atp synthase by nmr spectroscopy.
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Authors
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S.Wilkens,
D.Borchardt,
J.Weber,
A.E.Senior.
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Ref.
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Biochemistry, 2005,
44,
11786-11794.
[DOI no: ]
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PubMed id
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Abstract
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A critical point of interaction between F(1) and F(0) in the bacterial
F(1)F(0)-ATP synthase is formed by the alpha and delta subunits. Previous work
has shown that the N-terminal domain (residues 3-105) of the delta subunit forms
a 6 alpha-helix bundle [Wilkens, S., Dunn, S. D., Chandler, J., Dahlquist, F.
W., and Capaldi, R. A. (1997) Nat. Struct. Biol. 4, 198-201] and that the
majority of the binding energy between delta and F(1) is provided by the
interaction between the N-terminal 22 residues of the alpha- and N-terminal
domain of the delta subunit [Weber, J., Muharemagic, A., Wilke-Mounts, S., and
Senior, A. E. (2003) J. Biol. Chem. 278, 13623-13626]. We have now analyzed a
1:1 complex of the delta-subunit N-terminal domain and a peptide comprising the
N-terminal 22 residues of the alpha subunit by heteronuclear protein NMR
spectroscopy. A comparison of the chemical-shift values of delta-subunit
residues with and without alpha N-terminal peptide bound indicates that the
binding interface on the N-terminal domain of the delta subunit is formed by
alpha helices I and V. NOE cross-peak patterns in 2D (12)C/(12)C-filtered NOESY
spectra of the (13)C-labeled delta-subunit N-terminal domain in complex with
unlabeled peptide verify that residues 8-18 in the alpha-subunit N-terminal
peptide are folded as an alpha helix when bound to delta N-terminal domain. On
the basis of intermolecular contacts observed in (12)C/(13)C-filtered NOESY
experiments, we describe structural details of the interaction of the
delta-subunit N-terminal domain with the alpha-subunit N-terminal alpha helix.
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