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

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

doi:10.1002/anie.201106765

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 journal › Article › peer-review

40 Scopus citations

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. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Original language	English (US)
Pages (from-to)	1339-1342
Number of pages	4
Journal	Angewandte Chemie International Edition
Volume	51
Issue number	6
DOIs	https://doi.org/10.1002/anie.201106765
State	Published - Nov 16 2011
Externally published	Yes

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.

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title = "Crystal Structure of Methylornithine Synthase (PylB): Insights into the Pyrrolysine Biosynthesis",

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. Copyright {\textcopyright} 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.",

author = "Felix Quitterer and Anja List and Wolfgang Eisenreich and Adelbert Bacher and Michael Groll",

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.",

year = "2011",

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doi = "10.1002/anie.201106765",

language = "English (US)",

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T1 - Crystal Structure of Methylornithine Synthase (PylB): Insights into the Pyrrolysine Biosynthesis

AU - Quitterer, Felix

AU - List, Anja

AU - Eisenreich, Wolfgang

AU - Bacher, Adelbert

AU - Groll, Michael

N1 - 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.

PY - 2011/11/16

Y1 - 2011/11/16

N2 - 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.

AB - 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.

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JF - Angewandte Chemie International Edition

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

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