Structural insights into auxiliary cofactor usage by radical S-adenosylmethionine enzymes

Vivian Robert Jeyachandran, Amie K. Boal

Research output: Contribution to journalReview articlepeer-review

6 Scopus citations


Radical S-adenosylmethionine (SAM) enzymes use a common catalytic core for diverse transformations. While all radical SAM enzymes bind a Fe4S4 cluster via a characteristic tri-cysteine motif, many bind additional metal cofactors. Recently reported structures of radical SAM enzymes that use methylcobalamin or additional iron-sulfur clusters as cosubstrates show that these auxiliary units are anchored by N- and C-terminal domains that vary significantly in size and topology. Despite this architectural diversity, all use a common surface for auxiliary cofactor docking. In the sulfur insertion and metallocofactor assembly systems evaluated here, interaction with iron-sulfur cluster assembly proteins or downstream scaffold proteins is an important component of catalysis. Structures of these complexes represent important new frontiers in structural analysis of radical SAM enzymes.

Original languageEnglish (US)
Article number102153
JournalCurrent Opinion in Chemical Biology
StatePublished - Jun 2022

All Science Journal Classification (ASJC) codes

  • Analytical Chemistry
  • Biochemistry


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