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

Bibliographical note

KAUST Repository Item: Exported on 2020-10-01
Acknowledged KAUST grant number(s): FIC/2010/07
Acknowledgements: We thank Sophie Vieweg for experimental support and the staff of PXI of Paul Scherrer Institute, Swiss Light Source (Villigen, Switzerland) for help with data collection. This work was supported by the Hans-Fischer-Gesellschaft and by the King Abdullah University of Science and Technology (Award No. FIC/2010/07).
This publication acknowledges KAUST support, but has no KAUST affiliated authors.


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