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Crystal structure of human indoleamine 2,3-dioxygenase: Catalytic mechanism of O 2 incorporation by a heme-containing dioxygenase
Abstract
Human indoleamine 2,3-dioxygenase (IDO) catalyzes the cleavage of the pyrrol ring of l -Trp and incorporates both atoms of a molecule of oxygen (O 2 ). Here we report on the x-ray crystal structure of human IDO, complexed with the ligand inhibitor 4-phenylimidazole and cyanide. The overall structure of IDO shows two α-helical domains with the heme between them. A264 of the flexible loop in the heme distal side is in close proximity to the iron. A mutant analysis shows that none of the polar amino acid residues in the distal heme pocket are essential for activity, suggesting that, unlike the heme-containing monooxygenases (i.e., peroxidase and cytochrome P450), no protein group of IDO is essential in dioxygen activation or proton abstraction. These characteristics of the IDO structure provide support for a reaction mechanism involving the abstraction of a proton from the substrate by iron-bound dioxygen. Inactive mutants (F226A, F227A, and R231A) retain substrate-binding affinity, and an electron density map reveals that 2-( N -cyclohexylamino)ethane sulfonic acid is bound to these residues, mimicking the substrate. These findings suggest that strict shape complementarities between the indole ring of the substrate and the protein side chains are required, not for binding, but, rather, to permit the interaction between the substrate and iron-bound dioxygen in the first step of the reaction. This study provides the structural basis for a heme-containing dioxygenase mechanism, a missing piece in our understanding of heme chemistry.
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Indoleamine 2,3-dioxygenase 1 (IDO1) inhibitors in clinical trials for cancer immunotherapy
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The Role of Indoleamine 2, 3-Dioxygenase in Immune Suppression and Autoimmunity
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“Indoleamine 2, 3-dioxygenase (IDO) is a mammalian cytosolic enzyme composed of two alpha-helical domains with a heme group located between them responsible for catalyzing the initial step in tryptophan catabolism via the kynurenine degradation pathway [1] (Figure 1).”
Background
Metadata
- Authors
- Sugimoto, H., Oda, S.-I., Otsuki, T., Hino, T., Yoshida, T., & Shiro, Y.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2006-02-13
- Volume
- 103
- Issue
- 8
- Pages
- 2611-2616
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2152524078
- Cited by
- 441
- References
- 30
- FWCI
- 13.71
- Type
- journal article
- Language
- en
- Open access
- closed
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- Sugimoto, H., Oda, S.-I., Otsuki, T., Hino, T., Yoshida, T., & Shiro, Y. (2006). Crystal structure of human indoleamine 2,3-dioxygenase: Catalytic mechanism of O 2 incorporation by a heme-containing dioxygenase. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0508996103
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