PDBsum entry 2a7u

Hydrolase

PDB id: 2a7u

Contents

Protein chains

22 a.a.

105 a.a. *

* Residue conservation analysis

PDB id:

2a7u

Name:

Hydrolase

Title:

Nmr solution structure of the e.Coli f-atpase delta subunit n-terminal domain in complex with alpha subunit n-terminal 22 residues

Structure:

Atp synthase alpha chain. Chain: a. Fragment: n-terminal domain, (residues 1-22). Synonym: f-atpase alpha chain. Engineered: yes. Other_details: regulatory unit. Atp synthase delta chain. Chain: b. Fragment: n-terminal domain, (residues 2-135).

Source:

Synthetic: yes. Other_details: sequence occurs naturally in e.Coli, genes atpa, papa, unca. Escherichia coli. Organism_taxid: 83334. Strain: o157:h7. Gene: atph, pape, unch. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

1 models

Authors:

S.Wilkens,D.Borchardt,J.Weber,A.E.Senior

Key ref:

S.Wilkens et al. (2005). Structural characterization of the interaction of the delta and alpha subunits of the Escherichia coli F1F0-ATP synthase by NMR spectroscopy. Biochemistry, 44, 11786-11794. PubMed id: 16128580 DOI: 10.1021/bi0510678

Date:

06-Jul-05 Release date: 11-Oct-05

Protein chain

P0ABB2  (ATPA_ECO57) -  ATP synthase subunit alpha from Escherichia coli O157:H7

Seq: 513 a.a.

Struc: 22 a.a.

Protein chain

P0ABA5  (ATPD_ECO57) -  ATP synthase subunit delta from Escherichia coli O157:H7

Seq: 177 a.a.

Struc: 105 a.a.

Enzyme reactions

• Enzyme class 2: Chain A: E.C.7.1.2.2 - H(+)-transporting two-sector ATPase.
• Reaction: ATP + H2O + 4 H⁺(in) = ADP + phosphate + 5 H⁺(out)
• Enzyme class 3: Chain B: E.C.3.6.3.14 - Transferred entry: 7.1.2.2.
• Reaction: ATP + H₂O + H⁺(In) = ADP + phosphate + H⁺(Out)

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1021/bi0510678

Biochemistry 44:11786-11794 (2005)

PubMed id: 16128580

Structural characterization of the interaction of the delta and alpha subunits of the Escherichia coli F1F0-ATP synthase by NMR spectroscopy.

S.Wilkens, D.Borchardt, J.Weber, A.E.Senior.

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.