2a7u
From Proteopedia
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'''NMR solution structure of the E.coli F-ATPase delta subunit N-terminal domain in complex with alpha subunit N-terminal 22 residues''' | '''NMR solution structure of the E.coli F-ATPase delta subunit N-terminal domain in complex with alpha subunit N-terminal 22 residues''' | ||
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[[Category: ATP Synthase]] | [[Category: ATP Synthase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: H(+)-transporting two-sector ATPase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Borchardt, D.]] | [[Category: Borchardt, D.]] | ||
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[[Category: Weber, J.]] | [[Category: Weber, J.]] | ||
[[Category: Wilkens, S.]] | [[Category: Wilkens, S.]] | ||
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Revision as of 15:43, 3 May 2008
NMR solution structure of the E.coli F-ATPase delta subunit N-terminal domain in complex with alpha subunit N-terminal 22 residues
Overview
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.
About this Structure
2A7U is a Protein complex structure of sequences from Escherichia coli. The following page contains interesting information on the relation of 2A7U with [ATP Synthase]. Full crystallographic information is available from OCA.
Reference
Structural characterization of the interaction of the delta and alpha subunits of the Escherichia coli F1F0-ATP synthase by NMR spectroscopy., Wilkens S, Borchardt D, Weber J, Senior AE, Biochemistry. 2005 Sep 6;44(35):11786-94. PMID:16128580 Page seeded by OCA on Sat May 3 18:43:14 2008
