Structural highlights
Function
[UCRI_THEEB] Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions (By similarity).
Publication Abstract from PubMed
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 A 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.
Structure of a thermophilic cyanobacterial b(6)f-type Rieske protein.,Veit S, Takeda K, Tsunoyama Y, Rexroth D, Rogner M, Miki K Acta Crystallogr D Biol Crystallogr. 2012 Oct;68(Pt 10):1400-8. Epub 2012 Sep 18. PMID:22993094[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Veit S, Takeda K, Tsunoyama Y, Rexroth D, Rogner M, Miki K. Structure of a thermophilic cyanobacterial b(6)f-type Rieske protein. Acta Crystallogr D Biol Crystallogr. 2012 Oct;68(Pt 10):1400-8. Epub 2012 Sep 18. PMID:22993094 doi:http://dx.doi.org/10.1107/S0907444912034129
