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8CZP

2.25 angstrom resolution crystal structure of as-isolated KatG from Mycobacterium tuberculosis with an MYW cofactor

Summary for 8CZP
Entry DOI10.2210/pdb8czp/pdb
DescriptorCatalase-peroxidase, PROTOPORPHYRIN IX CONTAINING FE, ACETATE ION, ... (4 entities in total)
Functional Keywordsmet-tyr-trp cofactor, heme-dependent enzyme, oxidoreductase
Biological sourceMycobacterium tuberculosis
Total number of polymer chains2
Total formula weight162854.28
Authors
Li, J.,Liu, A. (deposition date: 2022-05-25, release date: 2023-12-13, Last modification date: 2024-10-23)
Primary citationLi, J.,Duan, R.,Traore, E.S.,Nguyen, R.C.,Davis, I.,Griffth, W.P.,Goodwin, D.C.,Jarzecki, A.A.,Liu, A.
Indole-N-Linked Hydroperoxyl Adduct of Protein-Derived Cofactor Modulating Catalase-Peroxidase Functions.
Angew.Chem.Int.Ed.Engl., :e202407018-e202407018, 2024
Cited by
PubMed Abstract: Bifunctional catalase-peroxidase (KatG) features a posttranslational methionine-tyrosine-tryptophan (MYW) crosslinked cofactor crucial for its catalase function, enabling pathogens to neutralize hydrogen peroxide during infection. We discovered the presence of indole nitrogen-linked hydroperoxyl adduct (MYW-OOH) in Mycobacterium tuberculosis KatG in the solution state under ambient conditions, suggesting its natural occurrence. By isolating predominantly MYW-OOH-containing KatG protein, we investigated the chemical stability and functional impact of MYW-OOH. We discovered that MYW-OOH inhibits catalase activity, presenting a unique temporary lock. Exposure to peroxide or increased temperature removes the hydroperoxyl adduct from the protein cofactor, converting MYW-OOH to MYW and restoring the detoxifying ability of the enzyme against hydrogen peroxide. Thus, the N-linked hydroperoxyl group is releasable. KatG with MYW-OOH represents a catalase dormant, but primed, state of the enzyme. These findings provide insight into chemical strategies targeting the bifunctional enzyme KatG in pathogens, highlighting the role of N-linked hydroperoxyl modifications in enzymatic function.
PubMed: 39300819
DOI: 10.1002/anie.202407018
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.25 Å)
Structure validation

239492

数据于2025-07-30公开中

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