Crystal Structure of Methylornithine Synthase (PylB): Insights into the Pyrrolysine Biosynthesis

Felix Quitterer, Anja List, Wolfgang Eisenreich, Adelbert Bacher, Michael Groll

Research output: Contribution to journalArticlepeer-review

39 Scopus citations


Made by the barrel load: The biosynthetic pathway of the recently discovered 22nd amino acid, pyrrolysine, starts with an isomerization of lysine to methylornithine, catalyzed by PylB. The X-ray crystal structure of PylB is determined (see picture) and shows it has a TIM barrel fold. The sealed central cavity contains a [4Fe-4S] cluster, S-adenosylmethionine (SAM), and methylornithine, whose 2R,3R configuration could be confirmed. The data suggest a fragmentation-recombination mechanism via a glycyl radical intermediate. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Original languageEnglish (US)
Pages (from-to)1339-1342
Number of pages4
JournalAngewandte Chemie International Edition
Issue number6
StatePublished - Nov 16 2011
Externally publishedYes


Dive into the research topics of 'Crystal Structure of Methylornithine Synthase (PylB): Insights into the Pyrrolysine Biosynthesis'. Together they form a unique fingerprint.

Cite this