Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8298601 | Biochimica et Biophysica Acta (BBA) - Bioenergetics | 2018 | 27 Pages |
Abstract
The binding site of the extrinsic protein PsbP in plant photosystem II was mapped by pulsed electron-electron double resonance, using mutant spinach PsbP (Pro20Cys, Ser82Cys, Ala111Cys, and Ala186Cys) labeled with 4-maleimido-TEMPO (MSL) spin label. The distances between the spin label and the Tyr160 neutral radical (YD) in PsbD, the D2 subunit of plant photosystem II, were 50.8â¯Â±â¯3.5â¯Ã
, 54.9â¯Â±â¯4.0â¯Ã
, 57.8â¯Â±â¯4.9â¯Ã
, and 58.4â¯Â±â¯14.1â¯Ã
, respectively. The geometry inferred from these distances was fitted to the PsbP crystal structure (PDB: 4RTI) to obtain the coordinates of YD relative to PsbP. These coordinates were then fitted under boundary conditions to the structure of cyanobacterial photosystem II (PDB: 4UB6), by rotating on Euler angles centered at fixed YD coordinates. The result proposed two models which show possible acidic amino acid residues in CP43, CP47 and D2 that can bind the basic amino acids Arg48, Lys143, and Lys160 in PsbP.
Keywords
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Mizue Asada, Taishi Nishimura, Kentaro Ifuku, Hiroyuki Mino,