Structural highlights
Function
CYC22_RHOCE Cytochrome c2 is found mainly in purple, non-sulfur, photosynthetic bacteria where it functions as the electron donor to the oxidized bacteriochlorophyll in the photophosphorylation pathway. However, it may also have a role in the respiratory chain and is found in some non-photosynthetic bacteria.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Cytochrome c(2) from the purple photosynthetic bacterium Rhodospirillum centenum has been crystallized by the sitting-drop vapour-diffusion method. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 29.7, b = 59.9, c = 65.4 A, and diffract to a resolution limit of 1.7 A. The Fe-atom position was determined from its anomalous scattering contribution and a molecular-replacement solution was calculated. The correctness of the solution was confirmed by parallel isomorphous replacement studies. The resulting model has a type I cytochrome fold with two features, an extended alpha-helix and a surface-charge distribution, that are distinctive to this protein. The implications of these structural features for the ability of the cytochrome to serve as an electron carrier are discussed.
Structure of cytochrome c2 from Rhodospirillum centenum.,Camara-Artigas A, Williams JC, Allen JP Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1498-505. Epub, 2001 Oct 25. PMID:11679712[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Camara-Artigas A, Williams JC, Allen JP. Structure of cytochrome c2 from Rhodospirillum centenum. Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1498-505. Epub, 2001 Oct 25. PMID:11679712
