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Crystal Structure of Methylornithine Synthase (PylB): Insights into the Pyrrolysine Biosynthesis
Author(s) -
Quitterer Felix,
List Anja,
Eisenreich Wolfgang,
Bacher Adelbert,
Groll Michael
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201106765
Subject(s) - biosynthesis , atp synthase , isomerization , crystal structure , stereochemistry , barrel (horology) , chemistry , amino acid , biochemistry , enzyme , crystallography , catalysis , materials science , composite material
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 2 R ,3 R configuration could be confirmed. The data suggest a fragmentation–recombination mechanism via a glycyl radical intermediate.