2A7U

NMR solution structure of the E.coli F-ATPase delta subunit N-terminal domain in complex with alpha subunit N-terminal 22 residues

Summary for 2A7U

• Entry DOI: 10.2210/pdb2a7u/pdb
• Related: 1ABV
• Descriptor: ATP synthase alpha chain, ATP synthase delta chain (2 entities in total)
• Functional Keywords: alpha helix bundle, hydrolase
• Biological source: Escherichia coli; More
• Cellular location: Cell inner membrane; Peripheral membrane protein: P00822 P0ABA4
• Total number of polymer chains: 2
• Total formula weight: 17240.50

Authors

Wilkens, S.,Borchardt, D.,Weber, J.,Senior, A.E. (deposition date: 2005-07-06, release date: 2005-10-11, Last modification date: 2024-05-01)

Primary citation

Wilkens, S.,Borchardt, D.,Weber, J.,Senior, A.E.
Structural Characterization of the Interaction of the delta and alpha Subunits of the Escherichia coli F(1)F(0)-ATP Synthase by NMR Spectroscopy
Biochemistry, 44:11786-11794, 2005

PubMed Abstract: 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.

PubMed: 16128580
DOI: 10.1021/bi0510678

Experimental method

SOLUTION NMR