Structure of cytochrome c2 from Rhodospirillum centenum.
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.
Camara-Artigas
A
A
Department of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287-1604, USA.
Williams
J C
JC
Allen
J P
JP
D003460:Crystallization; D018360:Crystallography, X-Ray; D003574:Cytochrome c Group / Q000737:chemistry*; D045362:Cytochromes c2; D008958:Models, Molecular; D011487:Protein Conformation; D012246:Rhodospirillum / Q000201:enzymology*
D003574:Cytochrome c Group; D045362:Cytochromes c2