Ontology highlight
ABSTRACT:
SUBMITTER: Koval T
PROVIDER: S-EPMC6757100 | biostudies-literature | 2019 Sep
REPOSITORIES: biostudies-literature
Kovaľ Tomáš T Švecová Leona L Østergaard Lars H LH Skalova Tereza T Dušková Jarmila J Hašek Jindřich J Kolenko Petr P Fejfarová Karla K Stránský Jan J Trundová Mária M Dohnálek Jan J
Scientific reports 20190923 1
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 presen ...[more]