Structural Insights into Radical Generation by the Radical SAM Superfamily

Table of Contents Table of Contents 1. Introduction 2. Unresolved Questions in the Radical SAM Enzyme Field 3. Highlighted Radical SAM Enzymes 3.1. Pyruvate Formate-Lyase Activating Enzyme (PFL-AE) 3.2. Oxygen-Independent Coproporphyrinogen III Oxidase (HemN)...

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Main Authors: Vey, Jessica Lynn, Drennan, Catherine L
Other Authors: Massachusetts Institute of Technology. Department of Biology
Format: Article
Language:en_US
Published: American Chemical Society 2012
Online Access:http://hdl.handle.net/1721.1/69646
https://orcid.org/0000-0001-5486-2755
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author Vey, Jessica Lynn
Drennan, Catherine L
author2 Massachusetts Institute of Technology. Department of Biology
author_facet Massachusetts Institute of Technology. Department of Biology
Vey, Jessica Lynn
Drennan, Catherine L
author_sort Vey, Jessica Lynn
collection MIT
description Table of Contents Table of Contents 1. Introduction 2. Unresolved Questions in the Radical SAM Enzyme Field 3. Highlighted Radical SAM Enzymes 3.1. Pyruvate Formate-Lyase Activating Enzyme (PFL-AE) 3.2. Oxygen-Independent Coproporphyrinogen III Oxidase (HemN) 3.3. Biotin Synthase (BioB) 3.4. Molybdenum Cofactor Biosynthesis Protein MoaA 3.5. Lysine Aminomutase (LAM) 3.6. Wye-Base Biosynthetic Protein TYW1 3.7. [Fe−Fe] Hydrogenase Maturase Protein HydE 4. Overall Fold 4.1. Radical SAM Core 4.2. Protein Elements Outside of the Radical SAM Core 5. FeS cluster 5.1. Location of the 4Fe−4S Cluster Binding Site 5.2. Environment Surrounding the Cluster 5.3. Interactions between the 4Fe−4S Cluster and AdoMet 6. AdoMet Binding 6.1. AdoMet Conformation 6.2. General Properties of the AdoMet Binding Site 6.3. Overall Description of the AdoMet Binding Site 6.3.1. AdoMet Methionyl Moiety 6.3.2. AdoMet Ribose 6.3.3. AdoMet Adenine Moiety 6.4. AdoMet Binding Motifs in the Radical SAM Superfamily 6.5. Deviations and Variations in AdoMet Binding between the Subfamilies 7. Implications of AdoMet Binding Site Architecture on Function and Reactivity 7.1. Tailoring the Reaction to Specific Substrates 7.2. AdoMet Usage as Cofactor or Cosubstrate 7.3. AdoMet Reaction Stoichiometry 7.4. HemN’s Second AdoMet (SAM2) 8. Substrate Binding to Radical SAM Enzymes 8.1. Positioning of the Substrate 8.2. Additional Cofactors in Some Radical SAM Substrate Binding Sites 8.3. Conformational Changes Associated with Substrate Binding in Radical SAM Enzymes 9. Reductant Binding in Radical SAM Enzymes 10. Other Known AdoMet-Binding Protein Folds 11. Conclusions
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spelling mit-1721.1/696462022-09-28T17:01:48Z Structural Insights into Radical Generation by the Radical SAM Superfamily Vey, Jessica Lynn Drennan, Catherine L Massachusetts Institute of Technology. Department of Biology Massachusetts Institute of Technology. Department of Chemistry Drennan, Catherine L. Drennan, Catherine L. Vey, Jessica L. Table of Contents Table of Contents 1. Introduction 2. Unresolved Questions in the Radical SAM Enzyme Field 3. Highlighted Radical SAM Enzymes 3.1. Pyruvate Formate-Lyase Activating Enzyme (PFL-AE) 3.2. Oxygen-Independent Coproporphyrinogen III Oxidase (HemN) 3.3. Biotin Synthase (BioB) 3.4. Molybdenum Cofactor Biosynthesis Protein MoaA 3.5. Lysine Aminomutase (LAM) 3.6. Wye-Base Biosynthetic Protein TYW1 3.7. [Fe−Fe] Hydrogenase Maturase Protein HydE 4. Overall Fold 4.1. Radical SAM Core 4.2. Protein Elements Outside of the Radical SAM Core 5. FeS cluster 5.1. Location of the 4Fe−4S Cluster Binding Site 5.2. Environment Surrounding the Cluster 5.3. Interactions between the 4Fe−4S Cluster and AdoMet 6. AdoMet Binding 6.1. AdoMet Conformation 6.2. General Properties of the AdoMet Binding Site 6.3. Overall Description of the AdoMet Binding Site 6.3.1. AdoMet Methionyl Moiety 6.3.2. AdoMet Ribose 6.3.3. AdoMet Adenine Moiety 6.4. AdoMet Binding Motifs in the Radical SAM Superfamily 6.5. Deviations and Variations in AdoMet Binding between the Subfamilies 7. Implications of AdoMet Binding Site Architecture on Function and Reactivity 7.1. Tailoring the Reaction to Specific Substrates 7.2. AdoMet Usage as Cofactor or Cosubstrate 7.3. AdoMet Reaction Stoichiometry 7.4. HemN’s Second AdoMet (SAM2) 8. Substrate Binding to Radical SAM Enzymes 8.1. Positioning of the Substrate 8.2. Additional Cofactors in Some Radical SAM Substrate Binding Sites 8.3. Conformational Changes Associated with Substrate Binding in Radical SAM Enzymes 9. Reductant Binding in Radical SAM Enzymes 10. Other Known AdoMet-Binding Protein Folds 11. Conclusions Massachusetts Institute of Technology (William Asbjornsen Albert Memorial Fellowship) Howard Hughes Medical Institute (Investigator) 2012-03-14T14:06:29Z 2012-03-14T14:06:29Z 2011-03 2009-07 Article http://purl.org/eprint/type/JournalArticle 0009-2665 1520-6890 http://hdl.handle.net/1721.1/69646 Vey, Jessica L., and Catherine L. Drennan. “Structural Insights into Radical Generation by the Radical SAM Superfamily.” Chemical Reviews 111.4 (2011): 2487–2506. https://orcid.org/0000-0001-5486-2755 en_US http://dx.doi.org/10.1021/cr9002616 Chemical Reviews Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. application/pdf American Chemical Society Prof. Drennan via Erja Kajosalo
spellingShingle Vey, Jessica Lynn
Drennan, Catherine L
Structural Insights into Radical Generation by the Radical SAM Superfamily
title Structural Insights into Radical Generation by the Radical SAM Superfamily
title_full Structural Insights into Radical Generation by the Radical SAM Superfamily
title_fullStr Structural Insights into Radical Generation by the Radical SAM Superfamily
title_full_unstemmed Structural Insights into Radical Generation by the Radical SAM Superfamily
title_short Structural Insights into Radical Generation by the Radical SAM Superfamily
title_sort structural insights into radical generation by the radical sam superfamily
url http://hdl.handle.net/1721.1/69646
https://orcid.org/0000-0001-5486-2755
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