Tuna cytochrome c at 2.0 A resolution. I.Ferricytochrome structure analysis

Autor: R. Swanson, Richard E. Dickerson, O.B. Kallai, B L Trus, N Mandel, G Mandel
Rok vydání: 1977
Předmět:
Zdroj: Journal of Biological Chemistry. 252:759-775
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)32783-7
Popis: The crystal structure of oxidized cytochrome c from tuna hearts has been solved by x-ray diffraction to a resolution of 2.0 A, using four isomorphous heavy atom derivatives. The crystals, space group P43, have 2 independent cytochrome molecules in the asymmetric repeating unit. No significant difference is seen between these 2 molecules, aside from conformations of a few surface side chains. The molecular folding observed is essentially that reported for tuna ferrocytochrome c. In particular, the ring of phenylalanine 83 lies against the heme group and closes the heme crevice, and is not swung out into the surroundings as had been believed from the 2.8 A horse ferricytochrome c structure.
Databáze: OpenAIRE