Role of the jelly-roll fold in substrate binding by 2-oxoglutarate oxygenases

Wei Shen Aik, Michael A McDonough, Armin Thalhammer, Rasheduzzaman Chowdhury, Christopher J Schofield*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

160 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)691-700
Number of pages10
JournalCurrent Opinion in Structural Biology
Issue number6
Publication statusPublished - Dec 2012

Scopus Subject Areas

  • Structural Biology
  • Molecular Biology


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