Disulfide linkage in the coiled-coil domain of subunit H of A(1)A(O) ATP synthase from Methanocaldococcus jannaschii and the NMR structure of the C-terminal segment H85-104

作者：Gayen Shovanlal; Grueber Gerhard

来源：FEBS Letters, 2010, 584(4): 713-718.

DOI：10.1016/j.febslet.2009.12.024

• Archaea
• A(1)A(O) ATP synthase
• ATP synthase
• Methanogen
• Subunit H
• Methanocaldococcus jannaschii

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 H85-104 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 H85-104, these results shine light into the A-H assembly of this enzyme.

• 出版日期2010-2-19
• 单位南阳理工学院