Basis for monomer stabilization in Rhodopseudomonas palustris cytochrome c' derived from the crystal structure.

@article{Shibata1998BasisFM,
  title={Basis for monomer stabilization in Rhodopseudomonas palustris cytochrome c' derived from the crystal structure.},
  author={Naoki Shibata and Satoru Iba and Shintaro Misaki and Terry E. Meyer and R. G. Bartsch and Michael A. Cusanovich and Yukio Morimoto and Yoshiki Higuchi and Noritake Yasuoka},
  journal={Journal of molecular biology},
  year={1998},
  volume={284 3},
  pages={751-60}
}
The crystal structure of an unusual monomeric cytochrome c' from Rhodopseudomonas palustris (RPCP) has been determined at 2.3 A resolution. RPCP has the four-helix (helices A, B, C and D) bundle structure similar to dimeric cytochromes c'. However the amino acid composition of the surface of helices A and B in RPCP is remarkably different from that of the dimeric cytochromes c'. This surface forms the dimer interface in the latter proteins. RPCP has seven charged residues on this surface… CONTINUE READING

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