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Rieske-type proteins structure

Only a few residues show more than 75% sequence identity, including four glycine residues, a proline residue at the beginning of the Pro loop, and a phenylalanine residue in a position corresponding to the conserved residue Tyr 165 of the bovine heart Rieske protein. However, structure prediction and sequence comparison with Rieske proteins from bci complexes suggests that the fold will be very similar in all Rieske-type ferredoxins, as in the other Rieske or Rieske-type proteins (see Section III,B,1). [Pg.89]

The Structures of Rieske and Rieske-Type Proteins Thomas A. Link... [Pg.650]

See other pages where Rieske-type proteins structure is mentioned: [Pg.83]    [Pg.84]    [Pg.85]    [Pg.85]    [Pg.87]    [Pg.89]    [Pg.91]    [Pg.93]    [Pg.95]    [Pg.97]    [Pg.99]    [Pg.100]    [Pg.101]    [Pg.103]    [Pg.105]    [Pg.105]    [Pg.107]    [Pg.109]    [Pg.111]    [Pg.113]    [Pg.115]    [Pg.117]    [Pg.119]    [Pg.121]    [Pg.123]    [Pg.127]    [Pg.129]    [Pg.131]    [Pg.133]    [Pg.135]    [Pg.137]    [Pg.139]    [Pg.141]    [Pg.143]    [Pg.143]    [Pg.145]    [Pg.147]    [Pg.149]    [Pg.151]    [Pg.151]    [Pg.153]    [Pg.155]    [Pg.157]   


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Protein structure types

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