Investigation of how gate residues in the main channel affect the catalytic activity of Scytalidium thermophilum catalase

Yuzugullu Karakus, Y.; Goc, G.; Zengin Karatas, M.; Balci Unver, S.; Yorke, B.A.; Pearson, A.R.

doi:10.1107/S2059798323011063

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 4
Main-channel architecture in recombinant wild-type CATPO (a) and its E484A (b), T188A (c) and T188F (d) variants in subunit A created using Caver. The channel in the T188A mutant is similar to that of wild-type CATPO, while in the E484A and T188F mutants the channel is disrupted and is likely to be effectively closed. The same is seen in all subunits. The insets show the shift in the position of Thr188 (cyan) and Phe188 (cyan) in the E484A (b) and T188F (d) variants compared with the corresponding position (Thr188, pink) in wild-type CATPO, respectively.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 80| Part 2| February 2024| Pages 101-112

https://doi.org/10.1107/S2059798323011063

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