Kristallstruktur der Methylornithin-Synthase (PylB): Einblicke in die Biosynthese von Pyrrolysin

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

Research output: Contribution to journalArticlepeer-review

Abstract

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.
Original languageEnglish (US)
Pages (from-to)1367-1370
Number of pages4
JournalAngewandte Chemie
Volume124
Issue number6
DOIs
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: Wir danken Sophie Vieweg fur ihre experimentelle Unterstutzung und den Mitarbeitern der PXI des Paul Scherrer Instituts, Swiss Light Source (Villigen, Schweiz) fur ihre Hilfe beim Messen der Datensutze. Diese Arbeit wurde von der Hans-Fischer-Gesellschaft und der King Abdullah University of Science and Technology (Award No. FIC/2010/07) gefçrdert.
This publication acknowledges KAUST support, but has no KAUST affiliated authors.

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