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- W1553864721 abstract "The structure of a low-potential [4Fe-4S]ferredoxin from Bacillus thermoproteolyticus has been solved using anomalous scattering data from iron atoms in the diffraction data of native crystals and refined partially to a crystallographic R-factor of 0.33, with 2.3 Å (1 Å = 0.1 nm) resolution data. The least-squares refinement based on the Bijvoet differences has determined that the four iron atoms in the cluster are an equal distance, approximately 2.8 Å, apart. The NH … S hydrogen bonds between polypeptide nitrogen atoms, and both cysteine and inorganic sulfur atoms, are present, as in ferredoxin from Peptococcus aerogenes. The polypeptide chain of the B. thermoproteolyticus ferredoxin has a fold closely similar to that of 2[4Fe-4S]ferredoxin from P. aerogenes. The structural correspondence indicates strongly that both types of ferredoxin evolved from a common ancestor. The second cluster-binding region in P. aerogenes ferredoxin corresponds to the α-helix in B. thermoproteolyticus ferredoxin. The secondary-structure predictions strongly suggest that the α-helix is generally present in the monocluster-type ferredoxins. The conformational change to α-helix, insertions of a loop and a protrusion, as well as the absence of the second cluster in B. thermoproteolyticus ferredoxin, result in the lack of 2-fold symmetry present in P. aerogenes ferredoxin. So, the track of gene duplication is no longer detectable in the tertiary structure alone. The evolutionary events that may have occurred in the ferredoxins with the [4Fe-4S]cluster are discussed." @default.
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- W1553864721 date "1988-01-01" @default.
- W1553864721 modified "2023-10-03" @default.
- W1553864721 title "Tertiary structure of Bacillus thermoproteolyticus [4Fe-4S] ferredoxin" @default.
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- W1553864721 doi "https://doi.org/10.1016/0022-2836(88)90388-9" @default.
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