1B9U
MEMBRANE DOMAIN OF THE SUBUNIT B OF THE E.COLI ATP SYNTHASE
Summary for 1B9U
| Entry DOI | 10.2210/pdb1b9u/pdb |
| Descriptor | PROTEIN (ATP SYNTHASE) (1 entity in total) |
| Functional Keywords | atp synthase, membrane protein, hydrolase |
| Cellular location | Cell inner membrane; Single-pass membrane protein (By similarity): P0ABA0 |
| Total number of polymer chains | 1 |
| Total formula weight | 3829.72 |
| Authors | Dmitriev, O.,Jones, P.C.,Jiang, W.,Fillingame, R.H. (deposition date: 1999-02-15, release date: 1999-09-15, Last modification date: 2023-11-15) |
| Primary citation | Dmitriev, O.,Jones, P.C.,Jiang, W.,Fillingame, R.H. Structure of the membrane domain of subunit b of the Escherichia coli F0F1 ATP synthase. J.Biol.Chem., 274:15598-15604, 1999 Cited by PubMed Abstract: The structure of the N-terminal transmembrane domain (residues 1-34) of subunit b of the Escherichia coli F0F1-ATP synthase has been solved by two-dimensional 1H NMR in a membrane mimetic solvent mixture of chloroform/methanol/H2O (4:4:1). Residues 4-22 form an alpha-helix, which is likely to span the hydrophobic domain of the lipid bilayer to anchor the largely hydrophilic subunit b in the membrane. The helical structure is interrupted by a rigid bend in the region of residues 23-26 with alpha-helical structure resuming at Pro-27 at an angle offset by 20 degrees from the transmembrane helix. In native subunit b, the hinge region and C-terminal alpha-helical segment would connect the transmembrane helix to the cytoplasmic domain. The transmembrane domains of the two subunit b in F0 were shown to be close to each other by cross-linking experiments in which single Cys were substituted for residues 2-21 of the native subunit and b-b dimer formation tested after oxidation with Cu(II)(phenanthroline)2. Cys residues that formed disulfide cross-links were found with a periodicity indicative of one face of an alpha-helix, over the span of residues 2-18, where Cys at positions 2, 6, and 10 formed dimers in highest yield. A model for the dimer is presented based upon the NMR structure and distance constraints from the cross-linking data. The transmembrane alpha-helices are positioned at a 23 degrees angle to each other with the side chains of Thr-6, Gln-10, Phe-14, and Phe-17 at the interface between subunits. The change in direction of helical packing at the hinge region may be important in the functional interaction of the cytoplasmic domains. PubMed: 10336456DOI: 10.1074/jbc.274.22.15598 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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