X-ray structure of an AdoMet radical activase reveals an anaerobic solution for formylglycine posttranslational modification (Q27678025)

1

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Tyler L Grove

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Lauren A Sites

3

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Martin I McLaughlin

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Squire J Booker

5

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Catherine L Drennan

Proceedings of the National Academy of Sciences of the United States of America

6

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language of work or name

English

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publication date

21 May 2013

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published in

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volume

110

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issue

21

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page(s)

8519-24

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cites work

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Structural Insights into Radical Generation by the Radical SAM Superfamily

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29 September 2017

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In vitro characterization of AtsB, a radical SAM formylglycine-generating enzyme that contains three [4Fe-4S] clusters

21 January 2018

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An anchoring role for FeS clusters: chelation of the amino acid moiety of S-adenosylmethionine to the unique iron site of the [4Fe-4S] cluster of pyruvate formate-lyase activating enzyme

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Anaerobic Sulfatase-Maturating Enzymes: Radical SAM Enzymes Able To Catalyze in Vitro Sulfatase Post-translational Modification

21 January 2018

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https://pubmed.ncbi.nlm.nih.gov/23650368

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

The Radical SAM Superfamily

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PubMed

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