title: Role of the jelly-roll fold in substrate binding by 2-oxoglutarate oxygenases.
abstract: 2-Oxoglutarate (2OG) and ferrous iron dependent oxygenases catalyze two-electron oxidations of a range of small and large molecule substrates, including proteins/peptides/amino acids, nucleic acids/bases, and lipids, as well as natural products including antibiotics and signaling molecules. 2OG oxygenases employ variations of a core double-stranded β-helix (DSBH; a.k.a. jelly-roll, cupin or jumonji C (JmjC)) fold to enable binding of Fe(II) and 2OG in a subfamily conserved manner. The topology of the DSBH limits regions directly involved in substrate binding: commonly the first, second and eighth strands, loops between the second/third and fourth/fifth DSBH strands, and the N-terminal and C-terminal regions are involved in primary substrate, co-substrate and cofactor binding. Insights into substrate recognition by 2OG oxygenases will help to enable selective inhibition and bioengineering studies.
authors.affiliation: Chemistry Research Laboratory, Mansfield Road, Oxford, OX1 3TA, United Kingdom.
authors.forename: WeiShen
authors.initials: W
authors.lastname: Aik
authors.forename: Michael A
authors.initials: MA
authors.lastname: McDonough
authors.forename: Armin
authors.initials: A
authors.lastname: Thalhammer
authors.forename: Rasheduzzaman
authors.initials: R
authors.lastname: Chowdhury
authors.forename: Christopher J
authors.initials: CJ
authors.lastname: Schofield
mesh_terms: D000818:Animals; D004791:Enzyme Inhibitors / Q000494:pharmacology; D006801:Humans; D010105:Oxygenases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D015202:Protein Engineering; D017433:Protein Structure, Secondary
chemical_list: D004791:Enzyme Inhibitors; D010105:Oxygenases