title: Disulfide linkage in the coiled-coil domain of subunit H of A1AO ATP synthase from Methanocaldococcus jannaschii and the NMR structure of the C-terminal segment H(85-104).
abstract: The C-terminal residues 98-104 are important for structure stability of subunit H of A(1)A(O) ATP synthases as well as its interaction with subunit A. Here we determined the structure of the segment H(85-104) of H from Methanocaldococcus jannaschii, showing a helix between residues Lys90 to Glu100 and flexible tails at both ends. The helix-helix arrangement in the C-terminus was investigated by exchange of hydrophobic residues to single cysteine in mutants of the entire subunit H (H(I93C), H(L96C) and H(L98C)). Together with the surface charge distribution of H(85-104), these results shine light into the A-H assembly of this enzyme.
authors.affiliation: School of Biological Sciences, Nanyang Technological University, Singapore, Republic of Singapore.
authors.forename: Shovanlal
authors.initials: S
authors.lastname: Gayen
authors.forename: Gerhard
authors.initials: G
authors.lastname: Grüber
mesh_terms: D019843:Archaeal Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D018360:Crystallography, X-Ray; D004220:Disulfides / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D017015:Methanococcales / Q000201:enzymology* / Q000235:genetics; D008958:Models, Molecular; D009154:Mutation; D011485:Protein Binding; D011487:Protein Conformation; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D019843:Archaeal Proteins; D004220:Disulfides; D021122:Protein Subunits; D006180:Proton-Translocating ATPases