Structure of a thermophilic cyanobacterial b(6)f-type Rieske protein
Veit, S., Takeda, K., Tsunoyama, Y., Rexroth, D., Rogner, M., Miki, K.(2012) Acta Crystallogr D Biol Crystallogr 68: 1400-1408
- PubMed: 22993094
- DOI: https://doi.org/10.1107/S0907444912034129
- Primary Citation of Related Structures:
3AZC - PubMed Abstract:
The `Rieske protein' PetC is one of the key subunits of the cytochrome b(6)f complex. Its Rieske-type [2Fe-2S] cluster participates in the photosynthetic electron-transport chain. Overexpression and careful structure analysis at 2.0 Å resolution of the extrinsic soluble domain of PetC from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1 enabled in-depth spectroscopic and structural characterization and suggested novel structural features. In particular, both the protein structure and the positions of the internal water molecules unexpectedly showed a higher similarity to eukaryotic PetCs than to other prokaryotic PetCs. The structure also revealed a deep pocket on the PetC surface which is oriented towards the membrane surface in the whole complex. Its surface properties suggest a binding site for a hydrophobic compound and the complete conservation of the pocket-forming residues in all known PetC sequences indicates the functional importance of this pocket in the cytochrome b(6)f complex.
Organizational Affiliation:
Plant Biochemistry, Ruhr University Bochum, 44780 Bochum, Germany.