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

Handle URI:
http://hdl.handle.net/10754/597905
Title:
Crystal Structure of Methylornithine Synthase (PylB): Insights into the Pyrrolysine Biosynthesis
Authors:
Quitterer, Felix; List, Anja; Eisenreich, Wolfgang; Bacher, Adelbert; Groll, Michael
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.
Citation:
Quitterer F, List A, Eisenreich W, Bacher A, Groll M (2011) Crystal Structure of Methylornithine Synthase (PylB): Insights into the Pyrrolysine Biosynthesis. Angew Chem Int Ed 51: 1339–1342. Available: http://dx.doi.org/10.1002/anie.201106765.
Publisher:
Wiley-Blackwell
Journal:
Angewandte Chemie International Edition
KAUST Grant Number:
FIC/2010/07
Issue Date:
16-Nov-2011
DOI:
10.1002/anie.201106765
PubMed ID:
22095926
Type:
Article
ISSN:
1433-7851
Sponsors:
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).
Appears in Collections:
Publications Acknowledging KAUST Support

Full metadata record

DC FieldValue Language
dc.contributor.authorQuitterer, Felixen
dc.contributor.authorList, Anjaen
dc.contributor.authorEisenreich, Wolfgangen
dc.contributor.authorBacher, Adelberten
dc.contributor.authorGroll, Michaelen
dc.date.accessioned2016-02-25T12:58:39Zen
dc.date.available2016-02-25T12:58:39Zen
dc.date.issued2011-11-16en
dc.identifier.citationQuitterer F, List A, Eisenreich W, Bacher A, Groll M (2011) Crystal Structure of Methylornithine Synthase (PylB): Insights into the Pyrrolysine Biosynthesis. Angew Chem Int Ed 51: 1339–1342. Available: http://dx.doi.org/10.1002/anie.201106765.en
dc.identifier.issn1433-7851en
dc.identifier.pmid22095926en
dc.identifier.doi10.1002/anie.201106765en
dc.identifier.urihttp://hdl.handle.net/10754/597905en
dc.description.abstractMade 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.en
dc.description.sponsorshipWe 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).en
dc.publisherWiley-Blackwellen
dc.subject(2R,3R)-3-methylornithineen
dc.subjectiron-sulfur proteinsen
dc.subjectMethanosarcina barkerien
dc.subjectPylB proteinen
dc.subjectpyrrolysineen
dc.titleCrystal Structure of Methylornithine Synthase (PylB): Insights into the Pyrrolysine Biosynthesisen
dc.typeArticleen
dc.identifier.journalAngewandte Chemie International Editionen
dc.contributor.institutionTechnische Universitat Munchen, Munich, Germanyen
kaust.grant.numberFIC/2010/07en

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