6i3k

Bilirubin oxidase from Myrothecium verrucaria, mutant W396A in complex with ferricyanide

spinqualitylabelsall models 6i3k, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6i3k is a 2 chain structure with sequence from Albifimbria verrucaria. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: BMA, CU, FC6, GOL, K, NA, NAG, PEG, SIN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BLRO_ALBVE Publication Abstract from PubMed Unlike any protein studied so far, the active site of bilirubin oxidase from Myrothecium verrucaria contains a unique type of covalent link between tryptophan and histidine side chains. The role of this post-translational modification in substrate binding and oxidation is not sufficiently understood. Our structural and mutational studies provide evidence that this Trp396-His398 adduct modifies T1 copper coordination and is an important part of the substrate binding and oxidation site. The presence of the adduct is crucial for oxidation of substituted phenols and it substantially influences the rate of oxidation of bilirubin. Additionally, we bring the first structure of bilirubin oxidase in complex with one of its products, ferricyanide ion, interacting with the modified tryptophan side chain, Arg356 and the active site-forming loop 393-398. The results imply that structurally and chemically distinct types of substrates, including bilirubin, utilize the Trp-His adduct mainly for binding and to a smaller extent for electron transfer. Trp-His covalent adduct in bilirubin oxidase is crucial for effective bilirubin binding but has a minor role in electron transfer.,Koval T, Svecova L, Ostergaard LH, Skalova T, Duskova J, Hasek J, Kolenko P, Fejfarova K, Stransky J, Trundova M, Dohnalek J Sci Rep. 2019 Sep 23;9(1):13700. doi: 10.1038/s41598-019-50105-3. PMID:31548583 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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