Defining the structural basis for assembly of a transmembrane cytochrome.

摘要: To define the structural basis for cofactor binding to membrane proteins, we introduce a manageable model system, which allows us, first time, study influence of individual transmembrane helices and single amino acid residues on assembly cytochrome. In vivo as well in vitro analyses indicate central roles either interaction or cofactor. The results clearly show that PsbF helix is independent from heme On other hand, highly depends helix-helix interactions. By site-directed mutagenesis critical were identified, are involved functional Especially, conserved glycine residue Based two-stage-model alpha-helical protein folding, presented third stage binds pre-assembled protein.