Background: KshA is a bacterial steroid-transforming oxygenase of biocatalytic interest and a virulence determinant in Mycobacterium tuberculosis. Results: Structures of KshA⅐steroid complexes were obtained for three homologs of different substrate specificity. Conclusion: Considerable structural flexibility contributes to the respective specificities of the different KshAs. Significance: This study provides insight into steroid catabolism and the conformational flexibility of Rieske oxygenases.

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