1ABV
N-TERMINAL DOMAIN OF THE DELTA SUBUNIT OF THE F1F0-ATP SYNTHASE FROM ESCHERICHIA COLI, NMR, MINIMIZED AVERAGE STRUCTURE
Summary for 1ABV
Entry DOI | 10.2210/pdb1abv/pdb |
Descriptor | DELTA SUBUNIT OF THE F1F0-ATP SYNTHASE (1 entity in total) |
Functional Keywords | atp synthesis, atp synthase, f1-atpase, delta subunit, nmr spectroscopy |
Biological source | Escherichia coli |
Total number of polymer chains | 1 |
Total formula weight | 14676.53 |
Authors | Wilkens, S.,Dunn, S.D.,Chandler, J.,Dahlquist, F.W.,Capaldi, R.A. (deposition date: 1997-01-29, release date: 1997-07-07, Last modification date: 2024-05-22) |
Primary citation | Wilkens, S.,Dunn, S.D.,Chandler, J.,Dahlquist, F.W.,Capaldi, R.A. Solution structure of the N-terminal domain of the delta subunit of the E. coli ATPsynthase. Nat.Struct.Biol., 4:198-201, 1997 Cited by PubMed Abstract: NMR studies of the delta subunit of the Escherichia coli F1F0-ATPsynthase reveal that it consists of an N-terminal six alpha-helix bundle and a less well ordered C terminus. Both domains are part of one of two separate connections between F1 and F0. PubMed: 9164460DOI: 10.1038/nsb0397-198 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
Download full validation report