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  • Title: Tuna cytochrome c at 2.0 A resolution. II. Ferrocytochrome structure analysis.
    Author: Takano T, Trus BL, Mandel N, Mandel G, Kallai OB, Swanson R, Dickerson RE.
    Journal: J Biol Chem; 1977 Jan 25; 252(2):776-85. PubMed ID: 188826.
    Abstract:
    The x-ray crystal structure analysis of tuna ferrocytochrome c has been extended from 2.45 to 2.0 A resolution. The overall folding is unchanged and is the same as has been reported for tuna ferricytochrome c (Swanson R., Trus, B.L., Mandel, N., Mandel, G., Kallai, O.B., and Dickerson, R.E. (1977) J. Biol. Chem. 252, 759-755). No significant structural differences are observed between oxidation states. Difference map studies using reoxidized crystals of ferrocytochrome c confirm the absence of a conformation change. A detailed analysis of hydrogen bonding shows the presence of six beta or 310 bends of type II with obligatory glycines in the 3rd residue position. This explains 6 of the 10 nearly invariant glycines in the molecule. Close packing contacts account for three more, and only the invariant glycine 1 remains a mystery.
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